메뉴 건너뛰기




Volumn 113, Issue , 2015, Pages 160-169

Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants

Author keywords

Comparative genomics; Glutamine transaminase; Maize; Methionine salvage pathway; Nicotiana tabacum cv. Bright Yellow 2; Poaceae; Solanaceae; Solanum lycopersicum cv. Floridade; Tobacco; Tomato; Yang cycle; Zea mays; Amidase

Indexed keywords


EID: 84899770320     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2014.04.012     Document Type: Article
Times cited : (23)

References (57)
  • 1
    • 77449131884 scopus 로고    scopus 로고
    • Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5′-methylthioadenosine
    • E. Albers Metabolic characteristics and importance of the universal methionine salvage pathway recycling methionine from 5′-methylthioadenosine IUBMB Life 61 2009 1132 1142
    • (2009) IUBMB Life , vol.61 , pp. 1132-1142
    • Albers, E.1
  • 2
    • 0019945865 scopus 로고
    • Identification of 2-keto-4-methylthiobutyrate as an intermediate in methionine synthesis from 5′-methylthioadenosine
    • P.S. Backlund Jr., C.P. Chang, and R.A. Smith Identification of 2-keto-4-methylthiobutyrate as an intermediate in methionine synthesis from 5′-methylthioadenosine J. Biol. Chem. 257 1982 4196 4202
    • (1982) J. Biol. Chem. , vol.257 , pp. 4196-4202
    • Backlund, Jr.P.S.1    Chang, C.P.2    Smith, R.A.3
  • 3
    • 0037384217 scopus 로고    scopus 로고
    • Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis
    • B.J. Berger, S. English, G. Chan, and M.H. Knodel Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis J. Bacteriol. 185 2003 2418 2431
    • (2003) J. Bacteriol. , vol.185 , pp. 2418-2431
    • Berger, B.J.1    English, S.2    Chan, G.3    Knodel, M.H.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 33646015669 scopus 로고    scopus 로고
    • The riboflavin transporter RibU in Lactococcus lactis: Molecular characterization of gene expression and the transport mechanism
    • C.M. Burgess, D.J. Slotboom, E.R. Geertsma, R.H. Duurkens, B. Poolman, and D. van Sinderen The riboflavin transporter RibU in Lactococcus lactis: molecular characterization of gene expression and the transport mechanism J. Bacteriol. 188 2006 2752 2760
    • (2006) J. Bacteriol. , vol.188 , pp. 2752-2760
    • Burgess, C.M.1    Slotboom, D.J.2    Geertsma, E.R.3    Duurkens, R.H.4    Poolman, B.5    Van Sinderen, D.6
  • 6
    • 77049322956 scopus 로고
    • Transamination of amino acids with glyoxylic acid in bacterial extracts
    • L.L. Campbell Jr. Transamination of amino acids with glyoxylic acid in bacterial extracts J. Bacteriol. 71 1956 81 83
    • (1956) J. Bacteriol. , vol.71 , pp. 81-83
    • Campbell, Jr.L.L.1
  • 7
    • 65349113784 scopus 로고    scopus 로고
    • Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis gamma-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate
    • S.M. Clark, R. Di Leo, P.K. Dhanoa, O.R. Van Cauwenberghe, R.T. Mullen, and B.J. Shelp Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis gamma-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate J. Exp. Bot. 60 2009 1743 1757
    • (2009) J. Exp. Bot. , vol.60 , pp. 1743-1757
    • Clark, S.M.1    Di Leo, R.2    Dhanoa, P.K.3    Van Cauwenberghe, O.R.4    Mullen, R.T.5    Shelp, B.J.6
  • 9
    • 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
    • C. Cobzaru, P. Ganas, M. Mihasan, P. Schleberger, and R. Brandsch 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 2011 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
  • 10
    • 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
    • A.J. Cooper 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 2004 557 577
    • (2004) Neurochem. Int. , vol.44 , pp. 557-577
    • Cooper, A.J.1
  • 11
    • 0022293332 scopus 로고
    • A-Keto acid omega-amidase from rat liver
    • A.J. Cooper, T.E. Duffy, and A. Meister A-Keto acid omega-amidase from rat liver Methods Enzymol. 113 1985 350 358
    • (1985) Methods Enzymol , vol.113 , pp. 350-358
    • Cooper, A.J.1    Duffy, T.E.2    Meister, A.3
  • 12
    • 0016155523 scopus 로고
    • Isolation and properties of a new glutamine transaminase from rat kidney
    • A.J. Cooper, and A. Meister Isolation and properties of a new glutamine transaminase from rat kidney J. Biol. Chem. 249 1974 2554 2561
    • (1974) J. Biol. Chem. , vol.249 , pp. 2554-2561
    • Cooper, A.J.1    Meister, A.2
  • 14
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • F. Corpet Multiple sequence alignment with hierarchical clustering Nucleic Acids Res. 16 1988 10881 10890
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 16
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP, and related tools
    • O. Emanuelsson, S. Brunak, G. von Heijne, and H. Nielsen Locating proteins in the cell using TargetP, SignalP, and related tools Nature Protoc. 2 2007 953 971
    • (2007) Nature Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 18
    • 0031593446 scopus 로고    scopus 로고
    • 13C nuclear magnetic resonance and gas chromatography to examine methionine catabolism by lactococci
    • 13C nuclear magnetic resonance and gas chromatography to examine methionine catabolism by lactococci Appl. Environ. Microbiol. 64 1998 4670 4675
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4670-4675
    • Gao, S.1    Mooberry, E.S.2    Steele, J.L.3
  • 20
    • 0026919907 scopus 로고
    • Efficient initiation of translation at non-AUG triplets in plant cells
    • K. Gordon, J. Fütterer, and T. Hohn Efficient initiation of translation at non-AUG triplets in plant cells Plant J. 2 1992 809 813
    • (1992) Plant J , vol.2 , pp. 809-813
    • Gordon, K.1    Fütterer, J.2    Hohn, T.3
  • 21
    • 72449145463 scopus 로고    scopus 로고
    • Unknown proteins and orphan enzymes: The missing half of the engineering parts list - And how to find it
    • A.D. Hanson, A. Pribat, J.C. Waller, and V. de Crécy-Lagard Unknown proteins and orphan enzymes: the missing half of the engineering parts list - and how to find it Biochem. J. 425 2009 1 11
    • (2009) Biochem. J. , vol.425 , pp. 1-11
    • Hanson, A.D.1    Pribat, A.2    Waller, J.C.3    De Crécy-Lagard, V.4
  • 22
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • K.L. Heckman, and L.R. Pease Gene splicing and mutagenesis by PCR-driven overlap extension Nat. Protoc. 2 2007 924 932
    • (2007) Nat. Protoc. , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 23
    • 0023058914 scopus 로고
    • Chromatographic analysis of the chiral and covalent instability of S-adenosyl-L-methionine
    • J.L. Hoffman Chromatographic analysis of the chiral and covalent instability of S-adenosyl-L-methionine Biochemistry 25 1986 4444 4449
    • (1986) Biochemistry , vol.25 , pp. 4444-4449
    • Hoffman, J.L.1
  • 24
    • 0035719739 scopus 로고    scopus 로고
    • Does glutamine act as a substrate for transamination reactions in the liver of fed and fasted sheep?
    • S.O. Hoskin, S. Gavet, E. Milne, and G.E. Lobley Does glutamine act as a substrate for transamination reactions in the liver of fed and fasted sheep? Br. J. Nutr. 85 2001 591 597
    • (2001) Br. J. Nutr. , vol.85 , pp. 591-597
    • Hoskin, S.O.1    Gavet, S.2    Milne, E.3    Lobley, G.E.4
  • 25
    • 1342304267 scopus 로고    scopus 로고
    • Glutamine:phenylpyruvate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • A. Hosono, H. Mizuguchi, H. Hayashi, M. Goto, I. Miyahara, K. Hirotsu, and H. Kagamiyama Glutamine:phenylpyruvate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 J. Biochem. 134 2003 843 851
    • (2003) J. Biochem. , vol.134 , pp. 843-851
    • Hosono, A.1    Mizuguchi, H.2    Hayashi, H.3    Goto, M.4    Miyahara, I.5    Hirotsu, K.6    Kagamiyama, H.7
  • 26
    • 85018015133 scopus 로고
    • Purification and characterization of two forms of glutamine amino-transferase from leaves of Pisum sativum
    • Y. Huang, and R.J. Ireland Purification and characterization of two forms of glutamine amino-transferase from leaves of Pisum sativum J. Exp. Bot. 42 1991 S61
    • (1991) J. Exp. Bot. , vol.42 , pp. S61
    • Huang, Y.1    Ireland, R.J.2
  • 27
    • 33645808723 scopus 로고    scopus 로고
    • An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants
    • A.O. Hudson, B.K. Singh, T. Leustek, and C. Gilvarg An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants Plant Physiol. 140 2006 292 301
    • (2006) Plant Physiol , vol.140 , pp. 292-301
    • Hudson, A.O.1    Singh, B.K.2    Leustek, T.3    Gilvarg, C.4
  • 28
    • 77049265670 scopus 로고
    • Estimation of α-keto acids in plant tissue: A critical study of various methods of extraction as applied to strawberry leaves, washed potato slices and peas
    • F.A. Isherwood, and C.A. Niavis Estimation of α-keto acids in plant tissue: a critical study of various methods of extraction as applied to strawberry leaves, washed potato slices and peas Biochem. J. 64 1956 549 558
    • (1956) Biochem. J. , vol.64 , pp. 549-558
    • Isherwood, F.A.1    Niavis, C.A.2
  • 29
    • 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
    • S. Jaisson, M. Veiga-da-Cunha, and E. Van Schaftingen Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2 Biochimie 91 2009 1066 1071
    • (2009) Biochimie , vol.91 , pp. 1066-1071
    • Jaisson, S.1    Veiga-Da-Cunha, M.2    Van Schaftingen, E.3
  • 30
    • 67651202156 scopus 로고    scopus 로고
    • Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination
    • B.F. Krasnikov, C.H. Chien, R. Nostramo, J.T. Pinto, E. Nieves, M. Callaway, J. Sun, K. Huebner, and A.J. Cooper Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination Biochimie 91 2009 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.9
  • 31
    • 57749113632 scopus 로고    scopus 로고
    • Arabidopsis peroxin11c-e, fission1b, and dynamin-related protein3A cooperate in cell cycle-associated replication of peroxisomes
    • M.J. Lingard, S.K. Gidda, S. Bingham, S.J. Rothstein, R.T. Mullen, and R.N. Trelease Arabidopsis peroxin11c-e, fission1b, and dynamin-related protein3A cooperate in cell cycle-associated replication of peroxisomes Plant Cell 20 2008 1567 1585
    • (2008) Plant Cell , vol.20 , pp. 1567-1585
    • Lingard, M.J.1    Gidda, S.K.2    Bingham, S.3    Rothstein, S.J.4    Mullen, R.T.5    Trelease, R.N.6
  • 32
    • 0017801792 scopus 로고
    • 2-Hydroxysuccinamic acid: A product of asparagine metabolism in plants
    • N.D. Lloyd, and K.W. Joy 2-Hydroxysuccinamic acid: a product of asparagine metabolism in plants Biochem. Biophys. Res. Commun. 81 1978 186 192
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 186-192
    • Lloyd, N.D.1    Joy, K.W.2
  • 33
    • 0001334704 scopus 로고
    • The methionine salvage pathway in relation to ethylene and polyamine biosynthesis
    • J.H. Miyazaki, and S.F. Yang The methionine salvage pathway in relation to ethylene and polyamine biosynthesis Physiol. Plant. 69 1987 366 370
    • (1987) Physiol. Plant. , vol.69 , pp. 366-370
    • Miyazaki, J.H.1    Yang, S.F.2
  • 34
    • 79951562208 scopus 로고    scopus 로고
    • ATTED-II updates: Condition-specific gene coexpression to extend coexpression analyses and applications to a broad range of flowering plants
    • T. Obayashi, K. Nishida, K. Kasahara, and K. Kinoshita ATTED-II updates: condition-specific gene coexpression to extend coexpression analyses and applications to a broad range of flowering plants Plant Cell Physiol. 52 2011 213 219
    • (2011) Plant Cell Physiol , vol.52 , pp. 213-219
    • Obayashi, T.1    Nishida, K.2    Kasahara, K.3    Kinoshita, K.4
  • 36
    • 0034123725 scopus 로고    scopus 로고
    • Branched-chain keto-acids and pyruvate in blood: Measurement by HPLC with fluorimetric detection and changes in older subjects
    • K. Pailla, F. Blonde-Cynober, C. Aussel, J.P. De Bandt, and L. Cynober Branched-chain keto-acids and pyruvate in blood: measurement by HPLC with fluorimetric detection and changes in older subjects Clin. Chem. 46 2000 848 853
    • (2000) Clin. Chem. , vol.46 , pp. 848-853
    • Pailla, K.1    Blonde-Cynober, F.2    Aussel, C.3    De Bandt, J.P.4    Cynober, L.5
  • 37
    • 0002151089 scopus 로고
    • Integrational Vectors for Genetic Manipulation in Bacillus subtilis
    • A.L. Sonenshein, J.A. Hoch, R. Losik, American Society for Microbiology Washington, DC
    • M. Perego Integrational Vectors for Genetic Manipulation in Bacillus subtilis A.L. Sonenshein, J.A. Hoch, R. Losik, Bacillus subtilis and other Gram-Positive Bacteria 1993 American Society for Microbiology Washington, DC 615 622
    • (1993) Bacillus Subtilis and Other Gram-Positive Bacteria , pp. 615-622
    • Perego, M.1
  • 38
    • 0037449739 scopus 로고    scopus 로고
    • Plant C-N hydrolases and the identification of a plant N-carbamoylputrescine amidohydrolase involved in polyamine biosynthesis
    • M. Piotrowski, T. Janowitz, and H. Kneifel Plant C-N hydrolases and the identification of a plant N-carbamoylputrescine amidohydrolase involved in polyamine biosynthesis J. Biol. Chem. 278 2002 1708 1712
    • (2002) J. Biol. Chem. , vol.278 , pp. 1708-1712
    • Piotrowski, M.1    Janowitz, T.2    Kneifel, H.3
  • 39
    • 48249141480 scopus 로고    scopus 로고
    • A complete inventory of all enzymes in the eukaryotic methionine salvage pathway
    • I. Pirkov, J. Norbeck, L. Gustafsson, and E. Albers A complete inventory of all enzymes in the eukaryotic methionine salvage pathway FEBS J. 275 2008 4111 4120
    • (2008) FEBS J , vol.275 , pp. 4111-4120
    • Pirkov, I.1    Norbeck, J.2    Gustafsson, L.3    Albers, E.4
  • 40
    • 0023266235 scopus 로고
    • Bioenergetic consequences of lactose starvation for continuously cultured Streptococcus cremoris
    • B. Poolman, E.J. Smid, H. Veldkamp, and W.N. Konings Bioenergetic consequences of lactose starvation for continuously cultured Streptococcus cremoris J. Bacteriol. 169 1987 1460 1468
    • (1987) J. Bacteriol. , vol.169 , pp. 1460-1468
    • Poolman, B.1    Smid, E.J.2    Veldkamp, H.3    Konings, W.N.4
  • 41
    • 79959824396 scopus 로고    scopus 로고
    • Phloem-specific expression of Yang cycle genes and identification of novel Yang cycle enzymes in Plantago and Arabidopsis
    • B. Pommerrenig, K. Feussner, W. Zierer, V. Rabinovych, F. Klebl, I. Feussner, and N. Sauer Phloem-specific expression of Yang cycle genes and identification of novel Yang cycle enzymes in Plantago and Arabidopsis Plant Cell 23 2011 1904 1919
    • (2011) Plant Cell , vol.23 , pp. 1904-1919
    • Pommerrenig, B.1    Feussner, K.2    Zierer, W.3    Rabinovych, V.4    Klebl, F.5    Feussner, I.6    Sauer, N.7
  • 42
    • 0028800634 scopus 로고
    • Methionine biosynthesis in higher plants. I. Purification and characterization of cystathionine gamma-synthase from spinach chloroplasts
    • S. Ravanel, M. Droux, and R. Douce Methionine biosynthesis in higher plants. I. Purification and characterization of cystathionine gamma-synthase from spinach chloroplasts Arch. Biochem. Biophys. 316 1995 572 584
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 572-584
    • Ravanel, S.1    Droux, M.2    Douce, R.3
  • 43
    • 0035999898 scopus 로고    scopus 로고
    • A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts
    • C. Rudhe, O. Chew, J. Whelan, and E. Glaser A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts Plant J. 30 2002 213 220
    • (2002) Plant J , vol.30 , pp. 213-220
    • Rudhe, C.1    Chew, O.2    Whelan, J.3    Glaser, E.4
  • 44
    • 16644385379 scopus 로고    scopus 로고
    • Functional analysis of methylthioribose kinase genes in plants
    • M. Sauter, K.A. Cornell, S. Beszteri, and G. Rzewuski Functional analysis of methylthioribose kinase genes in plants Plant Physiol. 136 2004 4061 4071
    • (2004) Plant Physiol , vol.136 , pp. 4061-4071
    • Sauter, M.1    Cornell, K.A.2    Beszteri, S.3    Rzewuski, G.4
  • 45
    • 33644846369 scopus 로고    scopus 로고
    • The immediate early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine
    • M. Sauter, R. Lorbiecke, B. Ouyang, T.C. Pochapsky, and G. Rzewuski The immediate early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine Plant J. 44 2005 718 729
    • (2005) Plant J , vol.44 , pp. 718-729
    • Sauter, M.1    Lorbiecke, R.2    Ouyang, B.3    Pochapsky, T.C.4    Rzewuski, G.5
  • 46
    • 0015818546 scopus 로고
    • 5′-Methylthioadenosine and related compounds as precursors of S-adenosylmethionine in yeast
    • F. Schlenk, C.R. Zydek-Cwick, and J.L. Dainko 5′-Methylthioadenosine and related compounds as precursors of S-adenosylmethionine in yeast Biochim. Biophys. Acta 320 1973 357 362
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 357-362
    • Schlenk, F.1    Zydek-Cwick, C.R.2    Dainko, J.L.3
  • 47
    • 19044362589 scopus 로고    scopus 로고
    • The methionine salvage pathway in Bacillus subtilis
    • A. Sekowska, and A. Danchin The methionine salvage pathway in Bacillus subtilis BMC Microbiol. 2 2002 8
    • (2002) BMC Microbiol , vol.2 , pp. 8
    • Sekowska, A.1    Danchin, A.2
  • 49
    • 0017760608 scopus 로고
    • Determination of pools of tricarboxylic acid cycle and related acids in bacteria
    • W.H. Siegel, T. Donohue, and R.W. Bernlohr Determination of pools of tricarboxylic acid cycle and related acids in bacteria Appl. Environ. Microbiol. 34 1977 512 517
    • (1977) Appl. Environ. Microbiol. , vol.34 , pp. 512-517
    • Siegel, W.H.1    Donohue, T.2    Bernlohr, R.W.3
  • 50
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • I. Small, N. Peeters, F. Legeai, and C. Lurin Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences Proteomics 4 2004 1581 1590
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 51
    • 0000132898 scopus 로고
    • Asparaginase and asparagine transaminase in soybean leaves and root nodules
    • J.G. Streeter Asparaginase and asparagine transaminase in soybean leaves and root nodules Plant Physiol. 60 1977 235 239
    • (1977) Plant Physiol , vol.60 , pp. 235-239
    • Streeter, J.G.1
  • 52
    • 62549096824 scopus 로고    scopus 로고
    • Participation of leaky ribosome scanning in protein dual targeting by alternative translation initiation in higher plants
    • Y. Wamboldt, S. Mohammed, C. Elowsky, C. Wittgren, W.B.M. de Paula, and S.A. Mackenzie Participation of leaky ribosome scanning in protein dual targeting by alternative translation initiation in higher plants Plant Cell 21 2009 157 167
    • (2009) Plant Cell , vol.21 , pp. 157-167
    • Wamboldt, Y.1    Mohammed, S.2    Elowsky, C.3    Wittgren, C.4    De Paula, W.B.M.5    MacKenzie, S.A.6
  • 53
    • 39749177631 scopus 로고    scopus 로고
    • Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding
    • I. Winge, J.A. McKinney, M. Ying, C.S. D'Santos, R. Kleppe, P.M. Knappskog, and J. Haavik Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding Biochem. J. 410 2008 195 204
    • (2008) Biochem. J. , vol.410 , pp. 195-204
    • Winge, I.1    McKinney, J.A.2    Ying, M.3    D'Santos, C.S.4    Kleppe, R.5    Knappskog, P.M.6    Haavik, J.7
  • 54
    • 79851516332 scopus 로고    scopus 로고
    • Dual targeting of mitochondrial proteins: Mechanism, regulation and function
    • O. Yogev, and O. Pines Dual targeting of mitochondrial proteins: mechanism, regulation and function Biochim. Biophys. Acta 1808 2011 1012 1020
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1012-1020
    • Yogev, O.1    Pines, O.2
  • 56
    • 84871318277 scopus 로고    scopus 로고
    • Characterization of Arabidopsis serine:glyoxylate aminotransferase, AGT1, as an asparagine aminotransferase
    • Q. Zhang, J. Lee, S. Pandurangan, M. Clarke, A. Pajak, and F. Marsolais Characterization of Arabidopsis serine:glyoxylate aminotransferase, AGT1, as an asparagine aminotransferase Phytochemistry 85 2013 30 35
    • (2013) Phytochemistry , vol.85 , pp. 30-35
    • Zhang, Q.1    Lee, J.2    Pandurangan, S.3    Clarke, M.4    Pajak, A.5    Marsolais, F.6
  • 57
    • 84894040431 scopus 로고    scopus 로고
    • Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis
    • Q. Zhang, and F. Marsolais Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis Phytochemistry 99 2014 36 43
    • (2014) Phytochemistry , vol.99 , pp. 36-43
    • Zhang, Q.1    Marsolais, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.