메뉴 건너뛰기




Volumn 185, Issue 15, 2003, Pages 4483-4489

Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; BACTERIAL ENZYME; EPIMERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SEA WATER; THREONINE; THREONINE 3 DEHYDROGENASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 0038444326     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.15.4483-4489.2003     Document Type: Article
Times cited : (28)

References (26)
  • 1
    • 0019877767 scopus 로고
    • L-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance
    • Aoyama, Y., and Y. Motokawa. 1981. L-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance. J. Biol. Chem. 256:12367-12373.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12367-12373
    • Aoyama, Y.1    Motokawa, Y.2
  • 2
    • 0024523884 scopus 로고
    • The primary structure of Escherichia coli L-threonine dehydrogenase
    • Aronson, B. D., R. L. Somerville, B. R. Epperly, and E. E. Dekker. 1989. The primary structure of Escherichia coli L-threonine dehydrogenase. J. Biol. Chem. 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
  • 3
    • 0023664631 scopus 로고
    • Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization
    • Asano, Y., A. Nakazawa, and K. Endo. 1987. Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization. J. Biol. Chem. 262:10346-10354.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10346-10354
    • Asano, Y.1    Nakazawa, A.2    Endo, K.3
  • 4
    • 0018181502 scopus 로고
    • L-threonine dehydrogenase of Escherichia coli K-12
    • Boylan, S. A., and E. E. Dekker. 1978. L-Threonine dehydrogenase of Escherichia coli K-12. Biochem. Biophys. Res. Commun. 85:190-197.
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 190-197
    • Boylan, S.A.1    Dekker, E.E.2
  • 5
    • 0019459723 scopus 로고
    • L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
    • Boylan, S. A., and E. E. Dekker. 1981. L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J. Biol. Chem. 256:1809-1815.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1809-1815
    • Boylan, S.A.1    Dekker, E.E.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0035941209 scopus 로고    scopus 로고
    • NADP-glutamate dehydrogenase isoenzymes of Saccharomyces cerevisiae. Purification, kinetic properties, and physiological roles
    • DeLuna, A., A. Avendano, L. Riego, and A. Gonzalez. 2001. NADP-glutamate dehydrogenase isoenzymes of Saccharomyces cerevisiae. Purification, kinetic properties, and physiological roles. J. Biol. Chem. 276:43775-43783.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43775-43783
    • DeLuna, A.1    Avendano, A.2    Riego, L.3    Gonzalez, A.4
  • 9
    • 0021701199 scopus 로고
    • Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase
    • Eklund, H., J. P. Samama, and T. A. Jones. 1984. Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Biochemistry 23:5982-5996.
    • (1984) Biochemistry , vol.23 , pp. 5982-5996
    • Eklund, H.1    Samama, J.P.2    Jones, T.A.3
  • 10
    • 0025847512 scopus 로고
    • L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies
    • Epperly, B. R., and E. E. Dekker. 1991. L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266:6086-6092.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6086-6092
    • Epperly, B.R.1    Dekker, E.E.2
  • 11
    • 0028518901 scopus 로고
    • Purification and structural characterization of porcine L-threonine dehydrogenase
    • Kao, Y. C., and L. Davis. 1994. Purification and structural characterization of porcine L-threonine dehydrogenase. Protein Expr. Purif. 5:423-431.
    • (1994) Protein Expr. Purif. , vol.5 , pp. 423-431
    • Kao, Y.C.1    Davis, L.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0014516037 scopus 로고
    • Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase"
    • McGilvray, D., and J. G. Morris. 1969. Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase." Biochem. J. 112:657-671.
    • (1969) Biochem. J. , vol.112 , pp. 657-671
    • McGilvray, D.1    Morris, J.G.2
  • 15
    • 0001596182 scopus 로고
    • Occurrence of D-threonine dehydrogenase in Pseudomonas cruciviae
    • Misono, H., Y. Shinagawa, S. Nagata, and S. Nagasaki. 1987. Occurrence of D-threonine dehydrogenase in Pseudomonas cruciviae. Agric. Biol. Chem. 51:1467-1469.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 1467-1469
    • Misono, H.1    Shinagawa, Y.2    Nagata, S.3    Nagasaki, S.4
  • 17
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • Morita, R. Y. 1975. Psychrophilic bacteria. Bacteriol. Rev. 39:144-167.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 18
    • 0018702816 scopus 로고
    • Purification and properties of alanine dehydrogenase from Bacillus sphaericus
    • Ohashima, T., and K. Soda. 1979. Purification and properties of alanine dehydrogenase from Bacillus sphaericus. Eur. J. Biochem. 100:29-30.
    • (1979) Eur. J. Biochem. , vol.100 , pp. 29-30
    • Ohashima, T.1    Soda, K.2
  • 19
    • 0017897436 scopus 로고
    • Properties of crystalline leucine dehydrogenase from Bacillus sphaericus
    • Ohshima, T., H. Misono, and K. Soda. 1978. Properties of crystalline leucine dehydrogenase from Bacillus sphaericus. J. Biol. Chem. 253:5719-5725.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5719-5725
    • Ohshima, T.1    Misono, H.2    Soda, K.3
  • 20
    • 0034825839 scopus 로고    scopus 로고
    • Psychrophilic valine dehydrogenase of the Antarctic psychrophile, Cytophaga sp. KUC-1: Purification, molecular characterization and expression
    • Oikawa, T., K. Yamanaka, T. Kazuoka, N. Kanzawa, and K. Soda. 2001. Psychrophilic valine dehydrogenase of the Antarctic psychrophile, Cytophaga sp. KUC-1: purification, molecular characterization and expression. Eur. J. Biochem. 268:4375-4383.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4375-4383
    • Oikawa, T.1    Yamanaka, K.2    Kazuoka, T.3    Kanzawa, N.4    Soda, K.5
  • 21
    • 0021796377 scopus 로고
    • L-threonine dehydrogenase from goat liver. Feedback inhibition by methylglyoxal
    • Ray, M., and S. Ray. 1985. L-Threonine dehydrogenase from goat liver. Feedback inhibition by methylglyoxal. J. Biol. Chem. 260:5913-5918.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5913-5918
    • Ray, M.1    Ray, S.2
  • 23
    • 0029849211 scopus 로고    scopus 로고
    • High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol
    • Thoden, J. B., P. A. Frey, and H. M. Holden. 1996. High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol. Protein Sci. 5:2149-2161.
    • (1996) Protein Sci. , vol.5 , pp. 2149-2161
    • Thoden, J.B.1    Frey, P.A.2    Holden, H.M.3
  • 24
    • 0034673977 scopus 로고    scopus 로고
    • Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase
    • Thoden, J. B., T. M. Wohlers, J. L. Fridovich-Keil, and H. M. Holden. 2000. Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry 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
  • 25
    • 0017079709 scopus 로고
    • A microgel system for disc electrophoresis
    • Tulchin, N., L. Ornstein, and B. J. Davis. 1976. A microgel system for disc electrophoresis. Anal. Biochem. 72:485-490.
    • (1976) Anal. Biochem. , vol.72 , pp. 485-490
    • Tulchin, N.1    Ornstein, L.2    Davis, B.J.3
  • 26
    • 0028932348 scopus 로고
    • Purification and characterization of threonine dehydrogenase from Clostridium sticklandii
    • Wagner, M., and J. R. Andreesen. 1995. Purification and characterization of threonine dehydrogenase from Clostridium sticklandii. Arch. Microbiol. 163:286-290.
    • (1995) Arch. Microbiol. , vol.163 , pp. 286-290
    • Wagner, M.1    Andreesen, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.