메뉴 건너뛰기




Volumn 3, Issue , 2002, Pages 1-12

Molecular cloning and tissue distribution of mammalian L-threonine3-dehydrogenases

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 3 KETOBUTYRATE COENZYME A; COMPLEMENTARY DNA; ENZYME; MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; THREONINE 3 DEHYDROGENASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 34248388102     PISSN: 14712091     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2091-3-19     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0035017459 scopus 로고    scopus 로고
    • Dietary supplements of mixtures of indispensable amino acids lacking threonine, phenylalanine or histidine increase the activity of hepatic threonine dehydrogenase, phenylalanine hydroxylase or histidase, respectively, and prevent growth depressions in chicks caused by dietary excesses of threonine, phenylalanine, or histidine
    • Keene JC, Austic RE: Dietary supplements of mixtures of indispensable amino acids lacking threonine, phenylalanine or histidine increase the activity of hepatic threonine dehydrogenase, phenylalanine hydroxylase or histidase, respectively, and prevent growth depressions in chicks caused by dietary excesses of threonine, phenylalanine, or histidine. J Nutr Biochem 2001, 12:274-284
    • (2001) J Nutr Biochem , vol.12 , pp. 274-284
    • Keene, J.C.1    Austic, R.E.2
  • 2
    • 0035461490 scopus 로고    scopus 로고
    • The effect of dietary protein level on threonine dehydrogenase activity in chickens
    • Yuan JH, Austic RE: The effect of dietary protein level on threonine dehydrogenase activity in chickens. Poult Sci 2001, 80:1353-1356
    • (2001) Poult Sci , vol.80 , pp. 1353-1356
    • Yuan, J.H.1    Austic, R.E.2
  • 3
    • 18244406583 scopus 로고    scopus 로고
    • A bioartificial liver - State of the art
    • Strain AJ, Neuberger JM: A bioartificial liver - state of the art. Science 2002, 295:1005-1009
    • (2002) Science , vol.295 , pp. 1005-1009
    • Strain, A.J.1    Neuberger, J.M.2
  • 4
    • 0018121957 scopus 로고
    • Catabolism of threonine in mammals by coupling of L-threonine 3-dehydrogenase with 2-amino-3-oxobutyrate-CoA ligase
    • Dale RA: Catabolism of threonine in mammals by coupling of L-threonine 3-dehydrogenase with 2-amino-3-oxobutyrate-CoA ligase. Biochim Biophys Acta 1978, 544:496-503
    • (1978) Biochim Biophys Acta , vol.544 , pp. 496-503
    • Dale, R.A.1
  • 5
    • 0019877767 scopus 로고
    • L-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance
    • Aoyama Y, Motokawa Y: L-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance. J Biol Chem 1981, 256:12367-12373
    • (1981) J Biol Chem , vol.256 , pp. 12367-12373
    • Aoyama, Y.1    Motokawa, Y.2
  • 6
    • 0020520189 scopus 로고
    • Metabolic homoeostasis of L-threonine in the normally-fed rat. Importance of liver threonine dehydrogenase activity
    • Bird MI, Nunn PB: Metabolic homoeostasis of L-threonine in the normally-fed rat. Importance of liver threonine dehydrogenase activity. Biochem J 1983, 214:687-694
    • (1983) Biochem J , vol.214 , pp. 687-694
    • Bird, M.I.1    Nunn, P.B.2
  • 7
    • 0023277621 scopus 로고
    • Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli
    • Ravnikar PD, Somerville RL: Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli. J Bacteriol 1987, 169:2611-2617
    • (1987) J Bacteriol , vol.169 , pp. 2611-2617
    • Ravnikar, P.D.1    Somerville, R.L.2
  • 8
    • 0019459723 scopus 로고
    • L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
    • Boylan SA, Dekker EE: L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J Biol Chem. 1981, 256:1809-1815
    • (1981) J Biol Chem , vol.256 , pp. 1809-1815
    • Boylan, S.A.1    Dekker, E.E.2
  • 10
    • 0022897006 scopus 로고
    • Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production
    • Tressel T, Thompson R, Zieske LR, Menendez MI, Davis L: Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production. J Biol Chem 1986, 261:16428-16437
    • (1986) J Biol Chem , vol.261 , pp. 16428-16437
    • Tressel, T.1    Thompson, R.2    Zieske, L.R.3    Menendez, M.I.4    Davis, L.5
  • 11
    • 0035340280 scopus 로고    scopus 로고
    • Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: Inferred reaction mechanism
    • Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, Cygler M: Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Biochemistry 2001, 40:5151-5160
    • (2001) Biochemistry , vol.40 , pp. 5151-5160
    • Schmidt, A.1    Sivaraman, J.2    Li, Y.3    Larocque, R.4    Barbosa, J.A.5    Smith, C.6    Matte, A.7    Schrag, J.D.8    Cygler, M.9
  • 12
    • 0034062775 scopus 로고    scopus 로고
    • Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs
    • Edgar AJ, Polak JM: Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur J Biochem 2000, 267:1805-1812
    • (2000) Eur J Biochem , vol.267 , pp. 1805-1812
    • Edgar, A.J.1    Polak, J.M.2
  • 13
    • 0032532659 scopus 로고    scopus 로고
    • Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38
    • Johnson AR, Chen YW, Dekker EE: Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38. Arch Biochem Biophys 1998, 358:211-221
    • (1998) Arch Biochem Biophys , vol.358 , pp. 211-221
    • Johnson, A.R.1    Chen, Y.W.2    Dekker, E.E.3
  • 14
    • 0028518901 scopus 로고
    • Purification and structural characterization of porcine L-threonine dehydrogenase
    • Kao YC, Davis L: Purification and structural characterization of porcine L-threonine dehydrogenase. Protein Expr Purif 1994, 5: 423-431
    • (1994) Protein Expr Purif , vol.5 , pp. 423-431
    • Kao, Y.C.1    Davis, L.2
  • 15
    • 0028932348 scopus 로고
    • Purification and characterization of threonine dehydrogenase from Clostridium sticklandii
    • Wagner M, Andreesen JR: Purification and characterization of threonine dehydrogenase from Clostridium sticklandii. Arch Microbiol 1995, 163:286-290
    • (1995) Arch Microbiol , vol.163 , pp. 286-290
    • Wagner, M.1    Andreesen, J.R.2
  • 17
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG, Vincens P: Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 1996, 241:779-786
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 18
    • 0013770885 scopus 로고
    • The enzymic formation of aminoacetone from threonine and its further metabolism
    • Green ML, Elliott WH: The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem J 1964, 92:537-549
    • (1964) Biochem J , vol.92 , pp. 537-549
    • Green, M.L.1    Elliott, W.H.2
  • 20
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 A resolution
    • Bauer AJ, Rayment I, Frey PA, Holden HM: The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 A resolution. Proteins 1992, 12:372-381
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 21
    • 0034673977 scopus 로고    scopus 로고
    • Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase
    • Thoden JB, Wohlers TM, Fridovich-Keil JL, HM Holden: Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry 2000, 39:5691-5701
    • (2000) Biochemistry , vol.39 , pp. 5691-5701
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 22
    • 0034934758 scopus 로고    scopus 로고
    • Characterization of hepatic L-threonine dehydrogenase of chicken
    • Yuan JH, Austic RE: Characterization of hepatic L-threonine dehydrogenase of chicken. Comp Biochem Physiol B Biochem Mol Biol 2001, 130:65-73
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.130 , pp. 65-73
    • Yuan, J.H.1    Austic, R.E.2
  • 23
    • 0024523884 scopus 로고
    • The primary structure of Escherichia coli L-threonine dehydrogenase
    • Aronson BD, Somerville RL, Epperly BR, Dekker EE: The primary structure of Escherichia coli L-threonine dehydrogenase. J Biol Chem 1989, 264:5226-5232
    • (1989) J Biol Chem , vol.264 , pp. 5226-5232
    • Aronson, B.D.1    Somerville, R.L.2    Epperly, B.R.3    Dekker, E.E.4
  • 24
    • 0031577155 scopus 로고    scopus 로고
    • Molecular characterization of the gene coding for threonine dehydrogenase in Xanthomonas campestris
    • Liu YS, Tseng YH, Lin JW, Weng SF: Molecular characterization of the gene coding for threonine dehydrogenase in Xanthomonas campestris. Biochem Biophys Res Commun 1997, 235:300-305
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 300-305
    • Liu, Y.S.1    Tseng, Y.H.2    Lin, J.W.3    Weng, S.F.4
  • 25
    • 0032188770 scopus 로고    scopus 로고
    • Nucleotide sequence, cloning, and overexpression of the D-threonine dehydrogenase gene from Pseudomonas cruciviae
    • Ashiuchi M, Packdibamrung K, Miyaji T, Nagata S, Misono H: Nucleotide sequence, cloning, and overexpression of the D-threonine dehydrogenase gene from Pseudomonas cruciviae. FEMS Microbiol Lett 1998, 167:75-80
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 75-80
    • Ashiuchi, M.1    Packdibamrung, K.2    Miyaji, T.3    Nagata, S.4    Misono, H.5
  • 26
    • 0030993736 scopus 로고    scopus 로고
    • Tissue localization of threonine oxidation in pigs
    • Le Floc'h N, Thibault JN, Seve B: Tissue localization of threonine oxidation in pigs. Br J Nutr 1997, 77:593-603
    • (1997) Br J Nutr , vol.77 , pp. 593-603
    • Le Floc'h, N.1    Thibault, J.N.2    Seve, B.3
  • 28
    • 0343611068 scopus 로고
    • Studies on the nature, inducibility, and assay of the threonine and serine dehydrase activities of rat liver
    • Goldstein L, Knox WE, Behrman EJ: Studies on the nature, inducibility, and assay of the threonine and serine dehydrase activities of rat liver. J Biol Chem 1962, 237:2855-2860
    • (1962) J Biol Chem , vol.237 , pp. 2855-2860
    • Goldstein, L.1    Knox, W.E.2    Behrman, E.J.3
  • 29
    • 0025082519 scopus 로고
    • Rat serine dehydratase gene codes for two species of mRNA of which only one is translated into serine dehydratase
    • Ogawa H, Fujioka M, Date T, Mueckler M, Su Y, Pitot HC: Rat serine dehydratase gene codes for two species of mRNA of which only one is translated into serine dehydratase. J Biol Chem 1990, 265:14407-14413
    • (1990) J Biol Chem , vol.265 , pp. 14407-14413
    • Ogawa, H.1    Fujioka, M.2    Date, T.3    Mueckler, M.4    Su, Y.5    Pitot, H.C.6
  • 30


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.