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Volumn 48, Issue 1, 2016, Pages 1-20

ω-Amidase: An underappreciated, but important enzyme in l-glutamine and l-asparagine metabolism; Relevance to sulfur and nitrogen metabolism, tumor biology and hyperammonemic diseases

Author keywords

Asparagine transaminase; Glutamine transaminase; Kynurenine aminotransferase; Nitrilase like protein (Nit2); Ketoglutaramate; Ketosuccinamate; Amidase

Indexed keywords

2 HYDROXYGLUTARIC ACID; 2 OXOGLUTARIC ACID; 2 OXOISOCAPROIC ACID; 4 HYDROXYBUTYRIC ACID; ALPHA AMINO ACID; AMIDASE; AMINOTRANSFERASE; ASPARAGINASE; ASPARAGINE; BIOLOGICAL MARKER; CASPASE 3; CYSTEINE CONJUGATE BETA LYASE; GLUTAMATE DEHYDROGENASE; GLUTAMINASE; GLUTAMINE; GLUTAMINE PHENYLPYRUVATE AMINOTRANSFERASE; GLUTAMINE TRANSAMINASE L; NITRILASE; NITRILASE LIKE PROTEIN 1; NITRILASE LIKE PROTEIN 2; OMEGA AMIDASE; OXALOACETIC ACID; SULFUR; UNCLASSIFIED DRUG; NITROGEN; OMEGA-AMIDASE;

EID: 84955201018     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-015-2061-7     Document Type: Review
Times cited : (46)

References (129)
  • 1
    • 0028932719 scopus 로고
    • Cloning and characterization of a soluble kynurenine aminotransferase from rat brain: Identity with kidney cysteine conjugate β-lyase
    • 7891071
    • Alberati-Giani D, Malherbe P, Köhler C, Lang G, Kiefer V, Lahm HW, Cesura AM (1995) Cloning and characterization of a soluble kynurenine aminotransferase from rat brain: identity with kidney cysteine conjugate β-lyase. J Neurochem 64:1448-1455
    • (1995) J Neurochem , vol.64 , pp. 1448-1455
    • Alberati-Giani, D.1    Malherbe, P.2    Köhler, C.3    Lang, G.4    Kiefer, V.5    Lahm, H.W.6    Cesura, A.M.7
  • 2
    • 0021908186 scopus 로고
    • Rat liver 4-hydroxy-2-ketoglutarate aldolase: Purification and kinetic characterization
    • 3966804
    • Anderson M, Scholtz JM, Schuster SM (1985) Rat liver 4-hydroxy-2-ketoglutarate aldolase: purification and kinetic characterization. Arch Biochem Biophys 236:82-97
    • (1985) Arch Biochem Biophys , vol.236 , pp. 82-97
    • Anderson, M.1    Scholtz, J.M.2    Schuster, S.M.3
  • 3
    • 0019420298 scopus 로고
    • Methionine synthesis from 5′-methylthioadenosine in rat liver
    • 7007366
    • Backlund PS Jr, Smith RA (1981) Methionine synthesis from 5′-methylthioadenosine in rat liver. J Biol Chem 256:1533-1535
    • (1981) J Biol Chem , vol.256 , pp. 1533-1535
    • Backlund, P.S.1    Smith, R.A.2
  • 5
    • 0003443846 scopus 로고
    • Verlag Chemie, Academic Press New York, London
    • Bergmeyer HU (ed) (1974) Methods of enzymatic analysis. Verlag Chemie, Academic Press, New York, London, pp 2285-2286
    • (1974) Methods of Enzymatic Analysis , pp. 2285-2286
    • Bergmeyer, H.U.1
  • 6
    • 0036909261 scopus 로고    scopus 로고
    • Catalysis in the nitrilase superfamily
    • 12504683
    • Brenner C (2002) Catalysis in the nitrilase superfamily. Curr Opin Struct Biol 12:775-782
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 775-782
    • Brenner, C.1
  • 7
    • 0026521259 scopus 로고
    • Kynurenine aminotransferase activity in human liver: Identity with human hepatic C-S lyase activity and a physiological role for this enzyme
    • 1595083
    • Buckberry LD, Blagbrough IS, Bycroft BW, Shaw PN (1992) Kynurenine aminotransferase activity in human liver: identity with human hepatic C-S lyase activity and a physiological role for this enzyme. Toxicol Lett 60:241-246
    • (1992) Toxicol Lett , vol.60 , pp. 241-246
    • Buckberry, L.D.1    Blagbrough, I.S.2    Bycroft, B.W.3    Shaw, P.N.4
  • 8
    • 84908505093 scopus 로고    scopus 로고
    • Pathophysiology of brain dysfunction in hyperammonemic syndromes: The many faces of glutamine
    • 25034052
    • Butterworth RF (2014) Pathophysiology of brain dysfunction in hyperammonemic syndromes: the many faces of glutamine. Mol Genet Metab 113:113-117
    • (2014) Mol Genet Metab , vol.113 , pp. 113-117
    • Butterworth, R.F.1
  • 9
    • 84872625904 scopus 로고
    • Acceleration of enzymatic desamidation of glutamine by several inorganic anions
    • 20257045
    • Carter CE, Greenstein JP (1947) Acceleration of enzymatic desamidation of glutamine by several inorganic anions. J Natl Cancer Inst 7:433-436
    • (1947) J Natl Cancer Inst , vol.7 , pp. 433-436
    • Carter, C.E.1    Greenstein, J.P.2
  • 11
    • 84864394097 scopus 로고    scopus 로고
    • Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: Kinetic assay and molecular dynamics simulation
    • 22674578 3406660
    • Chien CH, Gao QZ, Cooper AJ, Lyu JH, Sheu SY (2012) Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: kinetic assay and molecular dynamics simulation. J Biol Chem 287:25715-25726
    • (2012) J Biol Chem , vol.287 , pp. 25715-25726
    • Chien, C.H.1    Gao, Q.Z.2    Cooper, A.J.3    Lyu, J.H.4    Sheu, S.Y.5
  • 12
    • 0021353294 scopus 로고
    • Salvage of 5′-deoxy-methylthioadenosine into purines and methionine by lymphoid cells and inhibition of cell proliferation
    • 6421333
    • Christa L, Thuillier L, Munier A, Perignon JL (1984) Salvage of 5′-deoxy-methylthioadenosine into purines and methionine by lymphoid cells and inhibition of cell proliferation. Biochim Biophys Acta 803:7-10
    • (1984) Biochim Biophys Acta , vol.803 , pp. 7-10
    • Christa, L.1    Thuillier, L.2    Munier, A.3    Perignon, J.L.4
  • 13
    • 79952898929 scopus 로고    scopus 로고
    • Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria
    • 21288482
    • Cobzaru C, Ganas P, Mihasan M, Schleberger P, Brandsch R (2011) Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res Microbiol 162:285-291
    • (2011) Res Microbiol , vol.162 , pp. 285-291
    • Cobzaru, C.1    Ganas, P.2    Mihasan, M.3    Schleberger, P.4    Brandsch, R.5
  • 14
    • 0033912146 scopus 로고    scopus 로고
    • Bioactivation of selenocysteine Se-conjugates by a highly purified rat renal cysteine conjugate beta-lyase/glutamine transaminase K
    • 10900257
    • Commandeur JNM, Andreadou I, Rooseboom M, Out M, de Leur LJ, Groot E, Vermeulen NPE (2000) Bioactivation of selenocysteine Se-conjugates by a highly purified rat renal cysteine conjugate beta-lyase/glutamine transaminase K. J Pharmacol Exp Ther 294:753-761
    • (2000) J Pharmacol Exp Ther , vol.294 , pp. 753-761
    • Commandeur, J.N.M.1    Andreadou, I.2    Rooseboom, M.3    Out, M.4    De Leur, L.J.5    Groot, E.6    Vermeulen, N.P.E.7
  • 15
    • 85052769694 scopus 로고
    • Glutamine aminotransferases and ω-amidases
    • E. Kvamme (eds) 1 CRC Press Inc Boca Raton
    • Cooper AJL (1988) Glutamine aminotransferases and ω-amidases. In: Kvamme E (ed) Glutamine and glutamate in mammals, vol 1. CRC Press Inc, Boca Raton, pp 33-52
    • (1988) Glutamine and Glutamate in Mammals , pp. 33-52
    • Cooper, A.J.L.1
  • 16
    • 1542286199 scopus 로고    scopus 로고
    • The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants
    • 15016471
    • Cooper AJL (2004) The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants. Neurochem Int 44:557-577
    • (2004) Neurochem Int , vol.44 , pp. 557-577
    • Cooper, A.J.L.1
  • 17
    • 0015528204 scopus 로고
    • Isolation and properties of highly purified glutamine transaminase
    • 5059882
    • Cooper AJL, Meister A (1972) Isolation and properties of highly purified glutamine transaminase. Biochemistry 11:661-671
    • (1972) Biochemistry , vol.11 , pp. 661-671
    • Cooper, A.J.L.1    Meister, A.2
  • 18
    • 0016155523 scopus 로고
    • Isolation and properties of a new glutamine transaminase from rat kidney
    • 4822504
    • Cooper AJL, Meister A (1974) Isolation and properties of a new glutamine transaminase from rat kidney. J Biol Chem 249:2554-2561
    • (1974) J Biol Chem , vol.249 , pp. 2554-2561
    • Cooper, A.J.L.1    Meister, A.2
  • 19
    • 0000927503 scopus 로고
    • Comparative studies of glutamine transaminases from rat tissues
    • Cooper AJL, Meister A (1981) Comparative studies of glutamine transaminases from rat tissues. Comp Biochem Physiol 69B:137-145
    • (1981) Comp Biochem Physiol , vol.69 , pp. 137-145
    • Cooper, A.J.L.1    Meister, A.2
  • 21
    • 0023522337 scopus 로고
    • Fluorometric determination of α-ketosuccinamic acid in rat tissues
    • 3442326
    • Cooper AJ, Raps SP, Meister A (1987) Fluorometric determination of α-ketosuccinamic acid in rat tissues. Anal Biochem 167:312-320
    • (1987) Anal Biochem , vol.167 , pp. 312-320
    • Cooper, A.J.1    Raps, S.P.2    Meister, A.3
  • 22
    • 79960424466 scopus 로고    scopus 로고
    • Cysteine S-conjugate β-lyases: Important roles in the metabolism of naturally occurring sulfur and selenium-containing compounds, xenobiotics and anticancer agents
    • 20306345 2898922
    • Cooper AJL, Krasnikov BF, Niatsetskaya ZV, Pinto JT, Callery PS, Villar MT, Artigues A, Bruschi SA (2011) Cysteine S-conjugate β-lyases: important roles in the metabolism of naturally occurring sulfur and selenium-containing compounds, xenobiotics and anticancer agents. Amino Acids 41:7-27
    • (2011) Amino Acids , vol.41 , pp. 7-27
    • Cooper, A.J.L.1    Krasnikov, B.F.2    Niatsetskaya, Z.V.3    Pinto, J.T.4    Callery, P.S.5    Villar, M.T.6    Artigues, A.7    Bruschi, S.A.8
  • 23
    • 84944617256 scopus 로고    scopus 로고
    • Role of glutamine transaminases in nitrogen, sulfur, selenium and 1-carbon metabolism: Glutamine transaminases in normal and cancer cells
    • Rajendram R, Preedy VR, Patel VB (volume eds), A Bendich (series ed) Humana Press, New York
    • Cooper AJL, Dorai T, Dorai B, Krasnikov BF, Li J, Hallen A, and Pinto JT (2015) Role of glutamine transaminases in nitrogen, sulfur, selenium and 1-carbon metabolism: glutamine transaminases in normal and cancer cells. In: Rajendram R, Preedy VR, Patel VB (volume eds), A Bendich (series ed) Glutamine in clinical nutrition (nutrition and health series). Humana Press, New York, pp 37-54
    • (2015) Glutamine in Clinical Nutrition (Nutrition and Health Series) , pp. 37-54
    • Cooper, A.J.L.1    Dorai, T.2    Dorai, B.3    Krasnikov, B.F.4    Li, J.5    Hallen, A.6    Pinto, J.T.7
  • 24
    • 0022452954 scopus 로고
    • Glutamine and glutamate kinetics in humans
    • 2873746
    • Darmaun D, Matthews DE, Bier DM (1986) Glutamine and glutamate kinetics in humans. Am J Physiol 251:E117-E126
    • (1986) Am J Physiol , vol.251 , pp. E117-E126
    • Darmaun, D.1    Matthews, D.E.2    Bier, D.M.3
  • 26
    • 0016337327 scopus 로고
    • Identification of α-ketoglutaramate in rat liver, kidney, and brain. Relationship to glutamine transaminase and ω-amidase activities
    • 4436326
    • Duffy TE, Cooper AJL, Meister A (1974b) Identification of α-ketoglutaramate in rat liver, kidney, and brain. Relationship to glutamine transaminase and ω-amidase activities. J Biol Chem 249:7603-7606
    • (1974) J Biol Chem , vol.249 , pp. 7603-7606
    • Duffy, T.E.1    Cooper, A.J.L.2    Meister, A.3
  • 27
    • 79952140468 scopus 로고    scopus 로고
    • Folate and cancer: How DNA damage, repair and methylation impact on colon carcinogenesis
    • 20544289
    • Duthie SJ (2011) Folate and cancer: how DNA damage, repair and methylation impact on colon carcinogenesis. J Inherit Metab Dis 34:101-109
    • (2011) J Inherit Metab Dis , vol.34 , pp. 101-109
    • Duthie, S.J.1
  • 29
    • 84899770320 scopus 로고    scopus 로고
    • Evidence that glutamine transaminase and ω-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants
    • 24837359
    • Ellens KW, Richardson LG, Frelin O, Collins J, Ribeiro CL, Hsieh YF, Mullen RT, Hanson AD (2015) Evidence that glutamine transaminase and ω-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants. Phytochemistry 113:160-169
    • (2015) Phytochemistry , vol.113 , pp. 160-169
    • Ellens, K.W.1    Richardson, L.G.2    Frelin, O.3    Collins, J.4    Ribeiro, C.L.5    Hsieh, Y.F.6    Mullen, R.T.7    Hanson, A.D.8
  • 30
    • 79957991472 scopus 로고    scopus 로고
    • Glutaminase: A hot spot for regulation of cancer cell metabolism?
    • 21234284 3018840
    • Erickson JW, Cerione RA (2010) Glutaminase: a hot spot for regulation of cancer cell metabolism? Oncotarget 1:734-740
    • (2010) Oncotarget , vol.1 , pp. 734-740
    • Erickson, J.W.1    Cerione, R.A.2
  • 31
    • 84873793280 scopus 로고
    • Liver glutaminases
    • 18124173
    • Errera M (1949) Liver glutaminases. J Biol Chem 178:483-493
    • (1949) J Biol Chem , vol.178 , pp. 483-493
    • Errera, M.1
  • 32
    • 0010438306 scopus 로고
    • Desamidation of glutamine and asparagine in normal and neoplastic hepatic tissues
    • 20240440
    • Errera M, Greenstein JP (1947) Desamidation of glutamine and asparagine in normal and neoplastic hepatic tissues. J Natl Cancer Inst 7:285-288
    • (1947) J Natl Cancer Inst , vol.7 , pp. 285-288
    • Errera, M.1    Greenstein, J.P.2
  • 33
    • 0042945133 scopus 로고
    • Phosphate-activated glutaminase in kidney and other tissues
    • 18112132
    • Errera M, Greenstein JP (1949) Phosphate-activated glutaminase in kidney and other tissues. J Biol Chem 178:495-502
    • (1949) J Biol Chem , vol.178 , pp. 495-502
    • Errera, M.1    Greenstein, J.P.2
  • 34
    • 0015596134 scopus 로고
    • Concentrations of asparagine in tissues of prepubertal rats after enzymic or dietary depletion of asparagine
    • 4724595 1177631
    • Frankel DL, Wells H, Fillios LC (1973) Concentrations of asparagine in tissues of prepubertal rats after enzymic or dietary depletion of asparagine. Biochem J 132:645-648
    • (1973) Biochem J , vol.132 , pp. 645-648
    • Frankel, D.L.1    Wells, H.2    Fillios, L.C.3
  • 35
    • 6044244615 scopus 로고    scopus 로고
    • 'Conserved hypothetical' proteins: Prioritization of targets for experimental study
    • 15479782 524295
    • Galperin MY, Koonin EV (2004) 'Conserved hypothetical' proteins: prioritization of targets for experimental study. Nucleic Acids Res 32:5452-5463
    • (2004) Nucleic Acids Res , vol.32 , pp. 5452-5463
    • Galperin, M.Y.1    Koonin, E.V.2
  • 36
    • 0017646458 scopus 로고
    • The pathways of oxalate formation from phenylalanine, tyrosine, tryptophan and ascorbic acid in the rat
    • 889894
    • Gambardella RL, Richardson KE (1977) The pathways of oxalate formation from phenylalanine, tyrosine, tryptophan and ascorbic acid in the rat. Biochim Biophys Acta 499:156-168
    • (1977) Biochim Biophys Acta , vol.499 , pp. 156-168
    • Gambardella, R.L.1    Richardson, K.E.2
  • 37
    • 0018127894 scopus 로고
    • The formation of oxalate from hydroxypyruvate, serine, glycolate and glyoxylate in the rat
    • 719002
    • Gambardella RL, Richardson KE (1978) The formation of oxalate from hydroxypyruvate, serine, glycolate and glyoxylate in the rat. Biochim Biophys Acta 544:315-328
    • (1978) Biochim Biophys Acta , vol.544 , pp. 315-328
    • Gambardella, R.L.1    Richardson, K.E.2
  • 38
    • 84873784570 scopus 로고
    • Enzymatic desamidation of glutamine in the presence of pyruvate furnished by concomitant reactions
    • 20240437
    • Gonçalves JM, Greenstein JP (1947) Enzymatic desamidation of glutamine in the presence of pyruvate furnished by concomitant reactions. J Natl Cancer Inst 7:269-274
    • (1947) J Natl Cancer Inst , vol.7 , pp. 269-274
    • Gonçalves, J.M.1    Greenstein, J.P.2
  • 39
    • 84872622687 scopus 로고
    • Desamidation of amino acid amides in rat-liver extracts of varying concentrations
    • 20240439
    • Gonçalves JM, Price VE, Greenstein JP (1947) Desamidation of amino acid amides in rat-liver extracts of varying concentrations. J Natl Cancer Inst 7:281-284
    • (1947) J Natl Cancer Inst , vol.7 , pp. 281-284
    • Gonçalves, J.M.1    Price, V.E.2    Greenstein, J.P.3
  • 40
    • 0010484975 scopus 로고
    • Influence of α-keto acids on the desamidation of amino acid amides
    • 20280662
    • Greenstein JP, Carter CE (1946) Influence of α-keto acids on the desamidation of amino acid amides. J Natl Cancer Inst 7:57-60
    • (1946) J Natl Cancer Inst , vol.7 , pp. 57-60
    • Greenstein, J.P.1    Carter, C.E.2
  • 41
    • 78651009677 scopus 로고
    • α-Keto acid-activated glutaminase and asparaginase
    • 18116992
    • Greenstein JP, Price VE (1949) α-Keto acid-activated glutaminase and asparaginase. J Biol Chem 178:695-705
    • (1949) J Biol Chem , vol.178 , pp. 695-705
    • Greenstein, J.P.1    Price, V.E.2
  • 42
    • 34250156019 scopus 로고    scopus 로고
    • Mitochondrial aspartate aminotransferase: A third kynurenate-producing enzyme in the mammalian brain
    • 17442055
    • Guidetti P, Amori L, Sapko MT, Okuno E, Schwarcz R (2007) Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain. J Neurochem 102:103-111
    • (2007) J Neurochem , vol.102 , pp. 103-111
    • Guidetti, P.1    Amori, L.2    Sapko, M.T.3    Okuno, E.4    Schwarcz, R.5
  • 43
    • 11244258182 scopus 로고    scopus 로고
    • PH dependence, substrate specificity and inhibition of human kynurenine aminotransferase i
    • Han Q, Li J, Li J (2004) pH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I. Eur J Biochem 71:4804-4814
    • (2004) Eur J Biochem , vol.71 , pp. 4804-4814
    • Han, Q.1    Li, J.2    Li, J.3
  • 44
    • 57049172633 scopus 로고    scopus 로고
    • Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II
    • 18620547 2559858
    • Han Q, Cai T, Tagle DA, Robinson H, Li J (2008) Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II. Biosci Rep 28:205-215
    • (2008) Biosci Rep , vol.28 , pp. 205-215
    • Han, Q.1    Cai, T.2    Tagle, D.A.3    Robinson, H.4    Li, J.5
  • 45
    • 59249105861 scopus 로고    scopus 로고
    • Biochemical and structural properties of mouse kynurenine aminotransferase III
    • 19029248 2630683
    • Han Q, Robinson H, Cai T, Tagle DA, Li J (2009) Biochemical and structural properties of mouse kynurenine aminotransferase III. Mol Cell Biol 29:784-793
    • (2009) Mol Cell Biol , vol.29 , pp. 784-793
    • Han, Q.1    Robinson, H.2    Cai, T.3    Tagle, D.A.4    Li, J.5
  • 46
    • 0021847250 scopus 로고
    • Glutamine metabolism in isolated perfused rat liver. The transamination pathway
    • 2862885
    • Häussinger D, Stehle T, Gerok W (1985) Glutamine metabolism in isolated perfused rat liver. The transamination pathway. Biol Chem Hoppe Seyler 366:527-536
    • (1985) Biol Chem Hoppe Seyler , vol.366 , pp. 527-536
    • Häussinger, D.1    Stehle, T.2    Gerok, W.3
  • 47
    • 84919352181 scopus 로고    scopus 로고
    • Alternative functions of the brain transsulfuration pathway represent an underappreciated aspect of brain redox biochemistry with significant potential for therapeutic engagement
    • 25463282
    • Hensley K, Denton TT (2015) Alternative functions of the brain transsulfuration pathway represent an underappreciated aspect of brain redox biochemistry with significant potential for therapeutic engagement. Free Radic Biol Med 78:123-134
    • (2015) Free Radic Biol Med , vol.78 , pp. 123-134
    • Hensley, K.1    Denton, T.T.2
  • 48
    • 0015233819 scopus 로고
    • Rat liver ω-amidase. Purification and properties
    • 5114531
    • Hersh LB (1971) Rat liver ω-amidase. Purification and properties. Biochemistry 10:2884-2891
    • (1971) Biochemistry , vol.10 , pp. 2884-2891
    • Hersh, L.B.1
  • 49
    • 0015495890 scopus 로고
    • Rat liver ω -amidase. Kinetic evidence for an acyl-enzyme intermediate
    • 5028495
    • Hersh LB (1972) Rat liver ω -amidase. Kinetic evidence for an acyl-enzyme intermediate. Biochemistry 11:2251-2256
    • (1972) Biochemistry , vol.11 , pp. 2251-2256
    • Hersh, L.B.1
  • 50
    • 0027237014 scopus 로고
    • α-Keto and α-hydroxy branched-chain acid interrelationships in normal humans
    • 8360777
    • Hoffer LJ, Taveroff A, Robitaille L, Mamer OA, Reimer ML (1993) α-Keto and α-hydroxy branched-chain acid interrelationships in normal humans. J Nutr 123:1513-1521
    • (1993) J Nutr , vol.123 , pp. 1513-1521
    • Hoffer, L.J.1    Taveroff, A.2    Robitaille, L.3    Mamer, O.A.4    Reimer, M.L.5
  • 51
    • 0022859935 scopus 로고
    • Identity of rat liver mitochondrial asparagine-pyruvate transaminase with phenylalanine-pyruvate transaminase
    • 3106029
    • Hongo S, Ito H, Takeda M, Sato T (1986) Identity of rat liver mitochondrial asparagine-pyruvate transaminase with phenylalanine-pyruvate transaminase. Enzyme 36(4):232-238
    • (1986) Enzyme , vol.36 , Issue.4 , pp. 232-238
    • Hongo, S.1    Ito, H.2    Takeda, M.3    Sato, T.4
  • 53
    • 67651213552 scopus 로고    scopus 로고
    • Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2
    • 19596042
    • Jaisson S, Veiga-da-Cunha M, Van Schaftingen E (2009) Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2. Biochimie 91:1066-1071
    • (2009) Biochimie , vol.91 , pp. 1066-1071
    • Jaisson, S.1    Veiga-Da-Cunha, M.2    Van Schaftingen, E.3
  • 54
    • 0032507635 scopus 로고    scopus 로고
    • Reduced kynurenine aminotransferase-I activity in SHR rats may be due to lack of KAT-Ib activity
    • 9631442
    • Kapoor V, Thuruthyil SJ, Human B (1998) Reduced kynurenine aminotransferase-I activity in SHR rats may be due to lack of KAT-Ib activity. Neuroreport 9:1431-1444
    • (1998) Neuroreport , vol.9 , pp. 1431-1444
    • Kapoor, V.1    Thuruthyil, S.J.2    Human, B.3
  • 56
    • 67449126832 scopus 로고    scopus 로고
    • Assay and purification of ω-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the α-keto acid analogues of glutamine and asparagine
    • 19464248 2752201
    • Krasnikov BF, Nostramo R, Pinto JT, Cooper AJL (2009a) Assay and purification of ω-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the α-keto acid analogues of glutamine and asparagine. Anal Biochem 391:144-150
    • (2009) Anal Biochem , vol.391 , pp. 144-150
    • Krasnikov, B.F.1    Nostramo, R.2    Pinto, J.T.3    Cooper, A.J.L.4
  • 57
    • 67651202156 scopus 로고    scopus 로고
    • Identification of the putative tumor suppressor Nit2 as ω-amidase, an enzyme metabolically linked to glutamine and asparagine transamination
    • 19595734 2745200
    • Krasnikov BF, Chien CH, Nostramo R, Pinto JT, Nieves E, Callaway M, Sun J, Huebner K, Cooper AJL (2009b) Identification of the putative tumor suppressor Nit2 as ω-amidase, an enzyme metabolically linked to glutamine and asparagine transamination. Biochimie 91:1072-1080
    • (2009) Biochimie , vol.91 , pp. 1072-1080
    • Krasnikov, B.F.1    Chien, C.H.2    Nostramo, R.3    Pinto, J.T.4    Nieves, E.5    Callaway, M.6    Sun, J.7    Huebner, K.8    Cooper, A.J.L.9
  • 58
    • 79956273527 scopus 로고    scopus 로고
    • Urinary 2-hydroxy-5-oxoproline, the lactam form of α-ketoglutaramate, is markedly increased in urea cycle disorders
    • 21298421 3412270
    • Kuhara T, Inoue Y, Ohse M, Krasnikov BF, Cooper AJL (2011a) Urinary 2-hydroxy-5-oxoproline, the lactam form of α-ketoglutaramate, is markedly increased in urea cycle disorders. Anal Bioanal Chem 400:1843-1851
    • (2011) Anal Bioanal Chem , vol.400 , pp. 1843-1851
    • Kuhara, T.1    Inoue, Y.2    Ohse, M.3    Krasnikov, B.F.4    Cooper, A.J.L.5
  • 59
    • 79956264815 scopus 로고    scopus 로고
    • A GC/MS-based metabolomic approach for diagnosing citrin deficiency
    • 21365350
    • Kuhara T, Ohse M, Inoue Y, Cooper AJL (2011b) A GC/MS-based metabolomic approach for diagnosing citrin deficiency. Anal Bioanal Chem 400:1881-1894
    • (2011) Anal Bioanal Chem , vol.400 , pp. 1881-1894
    • Kuhara, T.1    Ohse, M.2    Inoue, Y.3    Cooper, A.J.L.4
  • 61
    • 34249048074 scopus 로고    scopus 로고
    • Growth inhibitory effect of the human NIT2 gene and its allelic imbalance in cancers
    • 17488281
    • Lin CH, Chung MY, Chen WB, Chien CH (2007) Growth inhibitory effect of the human NIT2 gene and its allelic imbalance in cancers. FEBS J 274:2946-2956
    • (2007) FEBS J , vol.274 , pp. 2946-2956
    • Lin, C.H.1    Chung, M.Y.2    Chen, W.B.3    Chien, C.H.4
  • 64
    • 0001215228 scopus 로고
    • Purification and properties of rat liver 2-keto-4-hydroxyglutarate aldolase
    • 14193832
    • Maitra U, Dekker EE (1964) Purification and properties of rat liver 2-keto-4-hydroxyglutarate aldolase. J Biol Chem 239:1485-1491
    • (1964) J Biol Chem , vol.239 , pp. 1485-1491
    • Maitra, U.1    Dekker, E.E.2
  • 65
    • 0029001375 scopus 로고
    • Identification of a mitochondrial form of kynurenine aminotransferase/glutamine transaminase K from rat brain
    • 7796908
    • Malherbe P, Alberati-Giani D, Köhler C, Cesura AM (1995) Identification of a mitochondrial form of kynurenine aminotransferase/glutamine transaminase K from rat brain. FEBS Lett 367:141-144
    • (1995) FEBS Lett , vol.367 , pp. 141-144
    • Malherbe, P.1    Alberati-Giani, D.2    Köhler, C.3    Cesura, A.M.4
  • 66
    • 0022462150 scopus 로고
    • Substrate metabolism of isolated jejunal epithelium: Conservation of three-carbon units
    • 3953776
    • Mallet RT, Kelleher JK, Jackson MJ (1986) Substrate metabolism of isolated jejunal epithelium: conservation of three-carbon units. Am J Physiol 250:C191-C198
    • (1986) Am J Physiol , vol.250 , pp. C191-C198
    • Mallet, R.T.1    Kelleher, J.K.2    Jackson, M.J.3
  • 67
    • 78651030210 scopus 로고
    • Preparation of enzymatic reactions of the keto analogues of asparagine and glutamine
    • 13034816
    • Meister A (1953) Preparation of enzymatic reactions of the keto analogues of asparagine and glutamine. J Biol Chem 200:571-589
    • (1953) J Biol Chem , vol.200 , pp. 571-589
    • Meister, A.1
  • 68
    • 0342425312 scopus 로고
    • Transamination from glutamine to α-keto acids
    • 14794702
    • Meister A, Tice SV (1950) Transamination from glutamine to α-keto acids. J Biol Chem 187:173-187
    • (1950) J Biol Chem , vol.187 , pp. 173-187
    • Meister, A.1    Tice, S.V.2
  • 69
    • 0011827520 scopus 로고
    • Transamination and associated deamidation of asparagine and glutamine
    • 12981062
    • Meister A, Sober HA, Tice SV, Fraser PE (1952) Transamination and associated deamidation of asparagine and glutamine. J Biol Chem 197:319-330
    • (1952) J Biol Chem , vol.197 , pp. 319-330
    • Meister, A.1    Sober, H.A.2    Tice, S.V.3    Fraser, P.E.4
  • 70
    • 0342769091 scopus 로고
    • Hydrolysis and transfer reactions catalyzed by ω-amidase preparations
    • 14392177
    • Meister A, Levintow L, Greenfield RE, Abendschein PA (1955) Hydrolysis and transfer reactions catalyzed by ω-amidase preparations. J Biol Chem 215:441-460
    • (1955) J Biol Chem , vol.215 , pp. 441-460
    • Meister, A.1    Levintow, L.2    Greenfield, R.E.3    Abendschein, P.A.4
  • 71
    • 0015239516 scopus 로고
    • Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase
    • 4396841
    • Miller JE, Litwack G (1971) Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase. J Biol Chem 246:3234-3240
    • (1971) J Biol Chem , vol.246 , pp. 3234-3240
    • Miller, J.E.1    Litwack, G.2
  • 72
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • 17287340 1794346
    • Molina H, Horn DM, Tang N, Mathivanan S, Pandey A (2007) Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 104:2199-2204
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 73
    • 84857236273 scopus 로고    scopus 로고
    • The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase
    • 22198249
    • Montioli R, Fargue S, Lewin J, Zamparelli C, Danpure CJ, Borri Voltattorni C, Cellini B (2012) The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase. Int J Biochem Cell Biol 44:536-546
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 536-546
    • Montioli, R.1    Fargue, S.2    Lewin, J.3    Zamparelli, C.4    Danpure, C.J.5    Borri Voltattorni, C.6    Cellini, B.7
  • 76
    • 2542625285 scopus 로고    scopus 로고
    • Deranged hypothetical proteins Rik protein, Nit protein 2 and mitochondrial inner membrane protein, Mitofilin, in fetal Down syndrome brain
    • Myung J, Gulesserian T, Fountoulakis M, Lubec G (2003) Deranged hypothetical proteins Rik protein, Nit protein 2 and mitochondrial inner membrane protein, Mitofilin, in fetal Down syndrome brain. Cell Mol Biol (Noisy-le-grand) 49:739-746
    • (2003) Cell Mol Biol (Noisy-le-grand) , vol.49 , pp. 739-746
    • Myung, J.1    Gulesserian, T.2    Fountoulakis, M.3    Lubec, G.4
  • 77
    • 0023928620 scopus 로고
    • Identification of mammalian aminotransferases utilizing glyoxylate or pyruvate as amino acceptor. Peroxisomal and mitochondrial asparagine aminotransferase
    • 3121607
    • Noguchi T, Fujiwara S (1988) Identification of mammalian aminotransferases utilizing glyoxylate or pyruvate as amino acceptor. Peroxisomal and mitochondrial asparagine aminotransferase. J Biol Chem 263:182-186
    • (1988) J Biol Chem , vol.263 , pp. 182-186
    • Noguchi, T.1    Fujiwara, S.2
  • 78
    • 0025771636 scopus 로고
    • Measurement of rat brain kynurenine aminotransferase at physiological kynurenine concentrations
    • 2072101
    • Okuno E, Schmidt W, Parks DA, Nakamura M, Schwarcz R (1991) Measurement of rat brain kynurenine aminotransferase at physiological kynurenine concentrations. J Neurochem 57:533-540
    • (1991) J Neurochem , vol.57 , pp. 533-540
    • Okuno, E.1    Schmidt, W.2    Parks, D.A.3    Nakamura, M.4    Schwarcz, R.5
  • 79
    • 0015392707 scopus 로고
    • The concentration of asparagine in the tissues of rats treated with growth hormone
    • 4643336 1174103
    • Ottaway JH (1972) The concentration of asparagine in the tissues of rats treated with growth hormone. Biochem J 129:503-505
    • (1972) Biochem J , vol.129 , pp. 503-505
    • Ottaway, J.H.1
  • 80
    • 0035114118 scopus 로고    scopus 로고
    • The nitrilase superfamily: Classification, structure and function
    • Pace HC, Brenner C (2001) The nitrilase superfamily: classification, structure and function. Genome Biol 2:1-9
    • (2001) Genome Biol , vol.2 , pp. 1-9
    • Pace, H.C.1    Brenner, C.2
  • 81
    • 0002726753 scopus 로고
    • Studies on the mechanism of glutamine synthesis; Isolation and properties of the enzyme from sheep brain
    • 14483465
    • Pamiljans V, Krishnaswamy PR, Dumville G, Meister A (1962) Studies on the mechanism of glutamine synthesis; isolation and properties of the enzyme from sheep brain. Biochemistry 1:153-158
    • (1962) Biochemistry , vol.1 , pp. 153-158
    • Pamiljans, V.1    Krishnaswamy, P.R.2    Dumville, G.3    Meister, A.4
  • 82
    • 84930378828 scopus 로고    scopus 로고
    • Glutaminase activity determines cytotoxicity of l-asparaginases on most leukemia cell lines
    • 25941002
    • Parmentier JH, Maggi M, Tarasco E, Scotti C, Avramis VI, Mittelman SD (2015) Glutaminase activity determines cytotoxicity of l-asparaginases on most leukemia cell lines. Leuk Res 39:757-762
    • (2015) Leuk Res , vol.39 , pp. 757-762
    • Parmentier, J.H.1    Maggi, M.2    Tarasco, E.3    Scotti, C.4    Avramis, V.I.5    Mittelman, S.D.6
  • 83
    • 0019230531 scopus 로고
    • The effect of the monocarboxylate translocator inhibitor, α-cyanocinnamate, on the oxidation of branched chain α-keto acids in rat liver
    • 7396523
    • Patel TB, Waymack PP, Olson MS (1980) The effect of the monocarboxylate translocator inhibitor, α-cyanocinnamate, on the oxidation of branched chain α-keto acids in rat liver. Arch Biochem Biophys 201:629-635
    • (1980) Arch Biochem Biophys , vol.201 , pp. 629-635
    • Patel, T.B.1    Waymack, P.P.2    Olson, M.S.3
  • 85
    • 0017714170 scopus 로고
    • Phosphate-dependent glutaminase of small intestine: Localization and role in intestinal glutamine metabolism
    • 900947
    • Pinkus LM, Windmueller HG (1977) Phosphate-dependent glutaminase of small intestine: localization and role in intestinal glutamine metabolism. Arch Biochem Biophys 182:506-517
    • (1977) Arch Biochem Biophys , vol.182 , pp. 506-517
    • Pinkus, L.M.1    Windmueller, H.G.2
  • 86
    • 84909957324 scopus 로고    scopus 로고
    • Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate β-lyase activity and can transaminate l-selenomethionine
    • 25231977 4223302
    • Pinto JT, Krasnikov BF, Alcutt S, Jones ME, Dorai T, Villar MT, Artigues A, Li J, Cooper AJL (2014) Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate β-lyase activity and can transaminate l-selenomethionine. J Biol Chem 289:30950-30961
    • (2014) J Biol Chem , vol.289 , pp. 30950-30961
    • Pinto, J.T.1    Krasnikov, B.F.2    Alcutt, S.3    Jones, M.E.4    Dorai, T.5    Villar, M.T.6    Artigues, A.7    Li, J.8    Cooper, A.J.L.9
  • 87
    • 4644336154 scopus 로고    scopus 로고
    • Glucose and glutamine utilization by rat lymphocytes, monocytes and neutrophils in culture: A comparative study
    • 15338472
    • Pithon-Curi TC, De Melo MP, Curi R (2004) Glucose and glutamine utilization by rat lymphocytes, monocytes and neutrophils in culture: a comparative study. Cell Biochem Funct 22:321-326
    • (2004) Cell Biochem Funct , vol.22 , pp. 321-326
    • Pithon-Curi, T.C.1    De Melo, M.P.2    Curi, R.3
  • 88
    • 77953617514 scopus 로고    scopus 로고
    • Reduction of endogenous kynurenic acid formation enhances extracellular glutamate, hippocampal plasticity, and cognitive behavior
    • 20336058 3055476
    • Potter MC, Elmer GI, Bergeron R, Albuquerque EX, Guidetti P, Wu HQ, Schwarcz R (2010) Reduction of endogenous kynurenic acid formation enhances extracellular glutamate, hippocampal plasticity, and cognitive behavior. Neuropsychopharmacology 35:1734-1742
    • (2010) Neuropsychopharmacology , vol.35 , pp. 1734-1742
    • Potter, M.C.1    Elmer, G.I.2    Bergeron, R.3    Albuquerque, E.X.4    Guidetti, P.5    Wu, H.Q.6    Schwarcz, R.7
  • 89
    • 84873785837 scopus 로고
    • Studies on the effect of pyruvate on the desamidation of glutamine, asparagine, and related compounds
    • 20240438
    • Price VE, Greenstein JP (1947) Studies on the effect of pyruvate on the desamidation of glutamine, asparagine, and related compounds. J Natl Cancer Inst 7:275-279
    • (1947) J Natl Cancer Inst , vol.7 , pp. 275-279
    • Price, V.E.1    Greenstein, J.P.2
  • 91
    • 84920890241 scopus 로고    scopus 로고
    • Increased plasma d-2-hydroxyglutarate in isocitrate dehydrogenase 2-mutated blastic plasmacytoid dendritic cell neoplasm
    • 25481493
    • Rakheja D, Fuda F, Vandergriff T, Boriack R, Medeiros BC, Frankel AE, Chen W (2015) Increased plasma d-2-hydroxyglutarate in isocitrate dehydrogenase 2-mutated blastic plasmacytoid dendritic cell neoplasm. Hum Pathol 46:322-326
    • (2015) Hum Pathol , vol.46 , pp. 322-326
    • Rakheja, D.1    Fuda, F.2    Vandergriff, T.3    Boriack, R.4    Medeiros, B.C.5    Frankel, A.E.6    Chen, W.7
  • 94
    • 84906536735 scopus 로고    scopus 로고
    • Cancer-associated isocitrate dehydrogenase 1 (IDH1) R132H mutation and d-2-hydroxyglutarate stimulate glutamine metabolism under hypoxia
    • 24986863 4156049
    • Reitman ZJ, Duncan CG, Poteet E, Winters A, Yan LJ, Gooden DM, Spasojevic I, Boros LG, Yang SH, Yan H (2014) Cancer-associated isocitrate dehydrogenase 1 (IDH1) R132H mutation and d-2-hydroxyglutarate stimulate glutamine metabolism under hypoxia. J Biol Chem 289:23318-23328
    • (2014) J Biol Chem , vol.289 , pp. 23318-23328
    • Reitman, Z.J.1    Duncan, C.G.2    Poteet, E.3    Winters, A.4    Yan, L.J.5    Gooden, D.M.6    Spasojevic, I.7    Boros, L.G.8    Yang, S.H.9    Yan, H.10
  • 96
    • 0019940133 scopus 로고
    • Utilization of nutrients by isolated epithelial cells of the rat colon
    • 7084619
    • Roediger WE (1982) Utilization of nutrients by isolated epithelial cells of the rat colon. Gastroenterology 83:424-429
    • (1982) Gastroenterology , vol.83 , pp. 424-429
    • Roediger, W.E.1
  • 97
    • 57049176460 scopus 로고    scopus 로고
    • Curiosity to kill the KAT (kynurenine aminotransferase): Structural insights into brain kynurenic acid synthesis
    • 18950711
    • Rossi F, Schwarcz R, Rizzi M (2008) Curiosity to kill the KAT (kynurenine aminotransferase): structural insights into brain kynurenic acid synthesis. Curr Opin Struct Biol 18:748-755
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 748-755
    • Rossi, F.1    Schwarcz, R.2    Rizzi, M.3
  • 101
    • 0036784518 scopus 로고    scopus 로고
    • Manipulation of brain kynurenines: Glial targets, neuronal effects, and clinical opportunities
    • 12235226
    • Schwarcz R, Pellicciari R (2002) Manipulation of brain kynurenines: glial targets, neuronal effects, and clinical opportunities. J Pharmacol Exp Ther 303:1-10
    • (2002) J Pharmacol Exp Ther , vol.303 , pp. 1-10
    • Schwarcz, R.1    Pellicciari, R.2
  • 103
    • 0015522899 scopus 로고
    • Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase
    • 4623131
    • Shrawder E, Martinez-Carrion M (1972) Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase. J Biol Chem 247:2486-2492
    • (1972) J Biol Chem , vol.247 , pp. 2486-2492
    • Shrawder, E.1    Martinez-Carrion, M.2
  • 104
    • 0347694257 scopus 로고
    • Amino transferases utilizing glyoxylate
    • Christen D.E. Metzler (eds) John Wiley and Sons New York
    • Smith IK (1985) Amino transferases utilizing glyoxylate. In: Christen P, Metzler DE (eds) Transaminases. John Wiley and Sons, New York, p 390
    • (1985) Transaminases , pp. 390
    • Smith, I.K.1
  • 106
    • 0022504397 scopus 로고
    • Blood-brain barrier transport of the alpha-keto acid analogs of amino acids
    • 3519290
    • Steele RD (1986) Blood-brain barrier transport of the alpha-keto acid analogs of amino acids. Fed Proc 45:2060-2064
    • (1986) Fed Proc , vol.45 , pp. 2060-2064
    • Steele, R.D.1
  • 107
    • 0015219154 scopus 로고
    • Structure of the dimeric α-keto acid analogue of asparagine
    • 5129723
    • Stephani RA, Meister A (1971) Structure of the dimeric α-keto acid analogue of asparagine. J Biol Chem 246:7115-7118
    • (1971) J Biol Chem , vol.246 , pp. 7115-7118
    • Stephani, R.A.1    Meister, A.2
  • 108
    • 0022979951 scopus 로고
    • A purified cysteine conjugate beta-lyase from rat kidney cytosol. Requirement for an alpha-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K
    • 3782077
    • Stevens JL, Robbins JD, Byrd RA (1986) A purified cysteine conjugate beta-lyase from rat kidney cytosol. Requirement for an alpha-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K. J Biol Chem 261:15529-15537
    • (1986) J Biol Chem , vol.261 , pp. 15529-15537
    • Stevens, J.L.1    Robbins, J.D.2    Byrd, R.A.3
  • 109
    • 0000132898 scopus 로고
    • Asparaginase and asparagine transaminase in soybean leaves and root nodules
    • 16660067 542587
    • Streeter JG (1977) Asparaginase and asparagine transaminase in soybean leaves and root nodules. Plant Physiol 60:235-239
    • (1977) Plant Physiol , vol.60 , pp. 235-239
    • Streeter, J.G.1
  • 110
    • 33645692860 scopus 로고    scopus 로고
    • D-2-Hydroxyglutaric aciduria: Unravelling the biochemical pathway and the genetic defect
    • 16601864
    • Struys EA (2006) d-2-Hydroxyglutaric aciduria: unravelling the biochemical pathway and the genetic defect. J Inherit Metab Dis 29:21-29
    • (2006) J Inherit Metab Dis , vol.29 , pp. 21-29
    • Struys, E.A.1
  • 111
    • 0000807680 scopus 로고
    • Amino Acid metabolism in pea leaves: Utilization of nitrogen from amide and amino groups of [N]asparagine
    • 16663517 1066775
    • Ta TC, Joy KW, Ireland RJ (1984a) Amino Acid metabolism in pea leaves: utilization of nitrogen from amide and amino groups of [N]asparagine. Plant Physiol 74:822-826
    • (1984) Plant Physiol , vol.74 , pp. 822-826
    • Ta, T.C.1    Joy, K.W.2    Ireland, R.J.3
  • 112
    • 84897680767 scopus 로고
    • Utilization of the amide groups of asparagine and 2-hydroxysuccinamic acid by young pea leaves
    • 16663659 1066948
    • Ta TC, Joy KW, Ireland RJ (1984b) Utilization of the amide groups of asparagine and 2-hydroxysuccinamic acid by young pea leaves. Plant Physiol 75:527-530
    • (1984) Plant Physiol , vol.75 , pp. 527-530
    • Ta, T.C.1    Joy, K.W.2    Ireland, R.J.3
  • 113
    • 0040388404 scopus 로고
    • Role of asparagine in the photorespiratory nitrogen metabolism of pea leaves
    • 16664240 1064730
    • Ta TC, Joy KW, Ireland RJ (1985) Role of asparagine in the photorespiratory nitrogen metabolism of pea leaves. Plant Physiol 78:334-337
    • (1985) Plant Physiol , vol.78 , pp. 334-337
    • Ta, T.C.1    Joy, K.W.2    Ireland, R.J.3
  • 114
    • 0015041887 scopus 로고
    • Regulation of rat liver glutamine synthetase: Activation by alpha-ketoglutarate and inhibition by glycine, alanine, and carbamyl phosphate
    • 5279520 389042
    • Tate SS, Meister A (1971) Regulation of rat liver glutamine synthetase: activation by alpha-ketoglutarate and inhibition by glycine, alanine, and carbamyl phosphate. Proc Natl Acad Sci USA 68:781-785
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 781-785
    • Tate, S.S.1    Meister, A.2
  • 115
    • 0016433855 scopus 로고
    • L-Kynurenine aminotransferase and l-α-aminoadipate aminotransferase. I. Evidence for identity
    • 1111529
    • Tobes MC, Mason M (1975) l-Kynurenine aminotransferase and l-α-aminoadipate aminotransferase. I. Evidence for identity. Biochem Biophys Res Commun 62:390-397
    • (1975) Biochem Biophys Res Commun , vol.62 , pp. 390-397
    • Tobes, M.C.1    Mason, M.2
  • 116
    • 0017744991 scopus 로고
    • α-Aminoadipate aminotransferase and kynurenine aminotransferase. Purification, characterization, and further evidence for identity
    • 873907
    • Tobes MC, Mason M (1977) α-Aminoadipate aminotransferase and kynurenine aminotransferase. Purification, characterization, and further evidence for identity. J Biol Chem 252:4591-4599
    • (1977) J Biol Chem , vol.252 , pp. 4591-4599
    • Tobes, M.C.1    Mason, M.2
  • 117
    • 64449084807 scopus 로고    scopus 로고
    • L: -2-Hydroxyglutaric aciduria, a disorder of metabolite repair
    • 19020988
    • Van Schaftingen E, Rzem R, Veiga-da-Cunha M (2009) L: -2-Hydroxyglutaric aciduria, a disorder of metabolite repair. J Inherit Metab Dis 32:135-142
    • (2009) J Inherit Metab Dis , vol.32 , pp. 135-142
    • Van Schaftingen, E.1    Rzem, R.2    Veiga-Da-Cunha, M.3
  • 119
    • 0015698053 scopus 로고
    • α-Ketoglutaramate, a neurotoxic agent in hepatic coma
    • 4788800
    • Vergara F, Duffy TE, Plum F (1973) α-Ketoglutaramate, a neurotoxic agent in hepatic coma. Trans Assoc Am Physicians 86:255-263
    • (1973) Trans Assoc Am Physicians , vol.86 , pp. 255-263
    • Vergara, F.1    Duffy, T.E.2    Plum, F.3
  • 120
    • 0015993253 scopus 로고
    • α-Ketoglutaramate: Increased concentrations in the cerebrospinal fluid of patients in hepatic coma
    • 4808789
    • Vergara F, Plum F, Duffy TE (1974) α-Ketoglutaramate: increased concentrations in the cerebrospinal fluid of patients in hepatic coma. Science 183:81-83
    • (1974) Science , vol.183 , pp. 81-83
    • Vergara, F.1    Plum, F.2    Duffy, T.E.3
  • 121
    • 0020023716 scopus 로고
    • Characterization of glutamine synthetase from avian liver mitochondria
    • 6126400
    • Vorhaben JE, Smith DD, Campbell JW (1982) Characterization of glutamine synthetase from avian liver mitochondria. Int J Biochem 14(8):747-756
    • (1982) Int J Biochem , vol.14 , Issue.8 , pp. 747-756
    • Vorhaben, J.E.1    Smith, D.D.2    Campbell, J.W.3
  • 122
    • 3042853805 scopus 로고    scopus 로고
    • Differential protein expression in MCF7 breast cancer cells transfected with ErbB2, neomycin resistance and luciferase plus yellow fluorescent protein
    • 15221777
    • Wang D, Jensen RH, Williams KE, Pallavicini MG (2004) Differential protein expression in MCF7 breast cancer cells transfected with ErbB2, neomycin resistance and luciferase plus yellow fluorescent protein. Proteomics 4:2175-2183
    • (2004) Proteomics , vol.4 , pp. 2175-2183
    • Wang, D.1    Jensen, R.H.2    Williams, K.E.3    Pallavicini, M.G.4
  • 123
    • 35348902569 scopus 로고    scopus 로고
    • Selenium in chemistry and biochemistry in comparison to sulfur
    • 17937613
    • Wessjohann LA, Schneider A, Abbas M, Brandt W (2007) Selenium in chemistry and biochemistry in comparison to sulfur. Biol Chem 388:997-1006
    • (2007) Biol Chem , vol.388 , pp. 997-1006
    • Wessjohann, L.A.1    Schneider, A.2    Abbas, M.3    Brandt, W.4
  • 124
    • 0028850881 scopus 로고
    • The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases
    • 7852397
    • Wray JW, Abeles RH (1995) The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J Biol Chem 270:3147-3153
    • (1995) J Biol Chem , vol.270 , pp. 3147-3153
    • Wray, J.W.1    Abeles, R.H.2
  • 125
    • 84895735874 scopus 로고    scopus 로고
    • Targeting kynurenine aminotransferase II in psychiatric diseases: Promising effects of an orally active enzyme inhibitor
    • 24562494 3934402
    • Wu HQ, Okuyama M, Kajii Y, Pocivavsek A, Bruno JP, Schwarcz R (2014) Targeting kynurenine aminotransferase II in psychiatric diseases: promising effects of an orally active enzyme inhibitor. Schizophr Bull 40(Suppl 2):S152-S158
    • (2014) Schizophr Bull , vol.40 , pp. S152-S158
    • Wu, H.Q.1    Okuyama, M.2    Kajii, Y.3    Pocivavsek, A.4    Bruno, J.P.5    Schwarcz, R.6
  • 126
    • 0030745596 scopus 로고    scopus 로고
    • Glutamine requirement of proliferating T lymphocytes
    • 9263257
    • Yaqoob P, Calder PC (1997) Glutamine requirement of proliferating T lymphocytes. Nutrition 13:646-651
    • (1997) Nutrition , vol.13 , pp. 646-651
    • Yaqoob, P.1    Calder, P.C.2
  • 127
    • 84894040431 scopus 로고    scopus 로고
    • Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis
    • 24461228
    • Zhang Q, Marsolais F (2014) Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis. Phytochemistry 99:36-43
    • (2014) Phytochemistry , vol.99 , pp. 36-43
    • Zhang, Q.1    Marsolais, F.2
  • 128
    • 84925448688 scopus 로고    scopus 로고
    • Downregulation of NIT2 inhibits colon cancer cell proliferation and induces cell cycle arrest through the caspase-3 and PARP pathways
    • 25738796
    • Zheng B, Chai R, Yu X (2015) Downregulation of NIT2 inhibits colon cancer cell proliferation and induces cell cycle arrest through the caspase-3 and PARP pathways. Int J Mol Med 35:1317-1322
    • (2015) Int J Mol Med , vol.35 , pp. 1317-1322
    • Zheng, B.1    Chai, R.2    Yu, X.3
  • 129
    • 0018257869 scopus 로고
    • Reciprocal regulation of glucose and glutamine utilization by cultured human diploid fibroblasts
    • 641112
    • Zielke HR, Ozand PT, Tildon JT, Sevdalian DA, Cornblath M (1978) Reciprocal regulation of glucose and glutamine utilization by cultured human diploid fibroblasts. J Cell Physiol 95:41-48
    • (1978) J Cell Physiol , vol.95 , pp. 41-48
    • Zielke, H.R.1    Ozand, P.T.2    Tildon, J.T.3    Sevdalian, D.A.4    Cornblath, M.5


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