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Volumn 410, Issue 1, 2011, Pages 44-56

Highly selective l-threonine 3-dehydrogenase from Cupriavidus necator and its use in determination of l-threonine

Author keywords

Cupriavidus necator; Endpoint assay; Enzymatic determination; l Threonine 3 dehydrogenase; Threonine determination

Indexed keywords

BLOOD; DIAGNOSIS; ENZYMES; METABOLISM; MICROORGANISMS; NITROGEN PLASMA; SCREENING; SUBSTRATES; ZINC;

EID: 78651352708     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.11.003     Document Type: Article
Times cited : (20)

References (57)
  • 1
    • 14944374472 scopus 로고    scopus 로고
    • Dietary threonine restriction specifically reduces intestinal mucin synthesis in rats
    • M. Faure, D. Moennoz, F. Montigon, C. Mettraux, D. Breuille, and O. Ballevre Dietary threonine restriction specifically reduces intestinal mucin synthesis in rats J. Nutr. 135 2005 486 491
    • (2005) J. Nutr. , vol.135 , pp. 486-491
    • Faure, M.1    Moennoz, D.2    Montigon, F.3    Mettraux, C.4    Breuille, D.5    Ballevre, O.6
  • 5
    • 34447116321 scopus 로고    scopus 로고
    • Threonine Utilization for synthesis of acute phase proteins, intestinal proteins, and mucins is increased during sepsis in rats
    • M. Faure, F. Chone, C. Mettraux, J.P. Godin, F. Bechereau, J. Vuichoud, I. Papet, D. Breuille, and C. Obled Threonine Utilization for synthesis of acute phase proteins, intestinal proteins, and mucins is increased during sepsis in rats J. Nutr. 137 2007 1802 1807
    • (2007) J. Nutr. , vol.137 , pp. 1802-1807
    • Faure, M.1    Chone, F.2    Mettraux, C.3    Godin, J.P.4    Bechereau, F.5    Vuichoud, J.6    Papet, I.7    Breuille, D.8    Obled, C.9
  • 6
    • 0018897754 scopus 로고
    • Induction of threonine imbalance by dispensable amino acids: Relationships between tissue amino acids and diet in rats
    • J.K. Tews, Y.L. Kim, and A.E. Harper Induction of threonine imbalance by dispensable amino acids: relationships between tissue amino acids and diet in rats J. Nutr. 110 1980 394 408
    • (1980) J. Nutr. , vol.110 , pp. 394-408
    • Tews, J.K.1    Kim, Y.L.2    Harper, A.E.3
  • 7
    • 2942709677 scopus 로고    scopus 로고
    • Nutritional considerations for vegetarian athletes
    • S.I. Barr, and C.A. Rideout Nutritional considerations for vegetarian athletes Nutrition 20 2004 696 703
    • (2004) Nutrition , vol.20 , pp. 696-703
    • Barr, S.I.1    Rideout, C.A.2
  • 9
    • 60449096560 scopus 로고    scopus 로고
    • A moderate threonine deficiency differently affects protein metabolism in tissues of early-weaned piglets
    • A. Hamard, B. Sve, and N. Le Floc'h A moderate threonine deficiency differently affects protein metabolism in tissues of early-weaned piglets Comp. Biochem. Physiol. A: Mol. Integr. Physiol. 152 2009 491 497
    • (2009) Comp. Biochem. Physiol. A: Mol. Integr. Physiol. , vol.152 , pp. 491-497
    • Hamard, A.1    Sve, B.2    Le Floc'H, N.3
  • 10
    • 33750813309 scopus 로고    scopus 로고
    • Application of an enzyme chip to the microquantification of L-phenylalanine
    • S. Tachibana, M. Suzuki, and Y. Asano Application of an enzyme chip to the microquantification of L-phenylalanine Anal. Biochem. 359 2006 72 78
    • (2006) Anal. Biochem. , vol.359 , pp. 72-78
    • Tachibana, S.1    Suzuki, M.2    Asano, Y.3
  • 11
    • 78651367235 scopus 로고
    • The microestimation of threonine
    • R.J. Block, and D. Bolling The microestimation of threonine J. Biol. Chem. 130 1939 365 374
    • (1939) J. Biol. Chem. , vol.130 , pp. 365-374
    • Block, R.J.1    Bolling, D.2
  • 12
    • 78651370814 scopus 로고
    • The determination of threonine by the use of periodate
    • L.A. Shin, and B.H. Nicolet The determination of threonine by the use of periodate J. Biol. Chem. 138 1941 91 96
    • (1941) J. Biol. Chem. , vol.138 , pp. 91-96
    • Shin, L.A.1    Nicolet, B.H.2
  • 13
    • 0035980439 scopus 로고    scopus 로고
    • Determination of eight essential amino acids in mixtures by chemometrics-spectrophotometry without separation
    • G. Fang, and N. Liu Determination of eight essential amino acids in mixtures by chemometrics-spectrophotometry without separation Anal. Chim. Acta 445 2001 245 253
    • (2001) Anal. Chim. Acta , vol.445 , pp. 245-253
    • Fang, G.1    Liu, N.2
  • 14
    • 78651363918 scopus 로고
    • Application of an immobilized Escherichia coli cell tube in analysis of L-threonine
    • K. Watanabe, N. Itoh, A. Tanaka, and S. Fukui Application of an immobilized Escherichia coli cell tube in analysis of L-threonine Agric. Biol. Chem. 46 1982 119 126
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 119-126
    • Watanabe, K.1    Itoh, N.2    Tanaka, A.3    Fukui, S.4
  • 15
    • 0017408147 scopus 로고
    • A specific method for the determination of threonine in rat blood plasma using aldehyde dehydrogenase
    • T. Nishida, S. Kume, M. Saito, and M. Suda A specific method for the determination of threonine in rat blood plasma using aldehyde dehydrogenase J. Biochem. 81 1977 1085 1090
    • (1977) J. Biochem. , vol.81 , pp. 1085-1090
    • Nishida, T.1    Kume, S.2    Saito, M.3    Suda, M.4
  • 16
    • 0017196568 scopus 로고
    • Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli
    • E.B. Newman, V. Kapoor, and R. Potter Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli J. Bacteriol. 126 1976 1245 1249
    • (1976) J. Bacteriol. , vol.126 , pp. 1245-1249
    • Newman, E.B.1    Kapoor, V.2    Potter, R.3
  • 17
    • 0034934758 scopus 로고    scopus 로고
    • Characterization of hepatic L-threonine dehydrogenase of chicken
    • J.H. Yuan, and R.E. Austic Characterization of hepatic L-threonine dehydrogenase of chicken Comp. Biochem. Physiol. 130 2001 65 73
    • (2001) Comp. Biochem. Physiol. , vol.130 , pp. 65-73
    • Yuan, J.H.1    Austic, R.E.2
  • 18
    • 0021796377 scopus 로고
    • L-Threonine dehydrogenase from goat liver
    • M. Ray, and S. Ray L-Threonine dehydrogenase from goat liver J. Biol. Chem. 260 1985 5916 5918
    • (1985) J. Biol. Chem. , vol.260 , pp. 5916-5918
    • Ray, M.1    Ray, S.2
  • 19
    • 0019877767 scopus 로고
    • L-Threonine dehydrogenase of chicken liver
    • Y. Aoyama, and Y. Motokawa L-Threonine dehydrogenase of chicken liver J. Biol. Chem. 256 1981 12367 12373
    • (1981) J. Biol. Chem. , vol.256 , pp. 12367-12373
    • Aoyama, Y.1    Motokawa, Y.2
  • 20
    • 3042609932 scopus 로고    scopus 로고
    • Threonine metabolism in Japanese quail liver
    • S. Akagi, K. Sato, and S. Ohmori Threonine metabolism in Japanese quail liver Amino acids 26 2004 235 242
    • (2004) Amino Acids , vol.26 , pp. 235-242
    • Akagi, S.1    Sato, K.2    Ohmori, S.3
  • 21
    • 34248388102 scopus 로고    scopus 로고
    • Molecular cloning and tissue distribution of mammalian L-threonine 3-dehydrogenases
    • A.J. Edgar Molecular cloning and tissue distribution of mammalian L-threonine 3-dehydrogenases BMC Biochem. 3 2002 19
    • (2002) BMC Biochem. , vol.3 , pp. 19
    • Edgar, A.J.1
  • 22
    • 0027284369 scopus 로고
    • PH-Dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization
    • J.P. Marcus, and E.E. Dekker pH-Dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization Biochem. Biophys. Res. Commun. 190 1993 1066 1072
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 1066-1072
    • Marcus, J.P.1    Dekker, E.E.2
  • 23
    • 0027363658 scopus 로고
    • Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase
    • J.P. Marcus, and E.E. Dekker Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase J. Bacteriol. 175 1993 6505 6511
    • (1993) J. Bacteriol. , vol.175 , pp. 6505-6511
    • Marcus, J.P.1    Dekker, E.E.2
  • 25
    • 0019459723 scopus 로고
    • L-Threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
    • S.A. Boylan, and E.E. Dekker L-Threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12 J. Biol. Chem. 256 1981 1809 1815
    • (1981) J. Biol. Chem. , vol.256 , pp. 1809-1815
    • Boylan, S.A.1    Dekker, E.E.2
  • 26
    • 0038444326 scopus 로고    scopus 로고
    • Novel Psychrophilic and thermolabile L-threonine dehydrogenase from Psychrophilic Cytophaga sp. strain KUC-1
    • T. Kazuoka, S. Takigawa, N. Arakawa, Y. Hizukuri, I. Muraoka, T. Oikawa, and K. Soda Novel Psychrophilic and thermolabile L-threonine dehydrogenase from Psychrophilic Cytophaga sp. strain KUC-1 J. Bacteriol. 15 2003 4483 4489
    • (2003) J. Bacteriol. , vol.15 , pp. 4483-4489
    • Kazuoka, T.1    Takigawa, S.2    Arakawa, N.3    Hizukuri, Y.4    Muraoka, I.5    Oikawa, T.6    Soda, K.7
  • 27
    • 0028932348 scopus 로고
    • Purification and characterization of threonine dehydrogenase from Clostridium sticklandii
    • M. Wagner, and J.R. Andreesen Purification and characterization of threonine dehydrogenase from Clostridium sticklandii Arch. Microbiol. 163 1995 286 290
    • (1995) Arch. Microbiol. , vol.163 , pp. 286-290
    • Wagner, M.1    Andreesen, J.R.2
  • 28
    • 33745272829 scopus 로고    scopus 로고
    • Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • R. Machielsen, and J. van der Oost Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus FEBS J. 273 2006 2722 2729
    • (2006) FEBS J. , vol.273 , pp. 2722-2729
    • MacHielsen, R.1    Van Der Oost, J.2
  • 29
    • 23944470849 scopus 로고    scopus 로고
    • L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: Gene cloning and enzymatic characterization
    • DOI 10.1007/s00792-005-0447-2
    • Y. Shimizu, H. Sakuraba, R. Kawakami, S. Goda, Y. Kawarabayasi, and T. Ohshima L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: gene cloning and enzymatic characterization Extremophiles 9 2005 317 324 (Pubitemid 41187700)
    • (2005) Extremophiles , vol.9 , Issue.4 , pp. 317-324
    • Shimizu, Y.1    Sakuraba, H.2    Kawakami, R.3    Goda, S.4    Kawarabayasi, Y.5    Ohshima, T.6
  • 30
    • 67651160661 scopus 로고    scopus 로고
    • Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Q. Bashir, N. Rashid, F. Jamil, T. Imanaka, and M. Akhtar Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis J. Biochem. 146 2009 95 102
    • (2009) J. Biochem. , vol.146 , pp. 95-102
    • Bashir, Q.1    Rashid, N.2    Jamil, F.3    Imanaka, T.4    Akhtar, M.5
  • 31
    • 62149125469 scopus 로고    scopus 로고
    • Biochemical characteristics and function of a threonine dehydrogenase encoded by ste11 in Ebosin biosynthesis of Streptomyces sp. 139
    • Y. Bao, H. Xie, J. Shan, R. Jiang, Y. Zhang, L. Guo, R. Zhang, and Y. Li Biochemical characteristics and function of a threonine dehydrogenase encoded by ste11 in Ebosin biosynthesis of Streptomyces sp. 139 J. Appl. Microbiol. 106 2009 1140 1146
    • (2009) J. Appl. Microbiol. , vol.106 , pp. 1140-1146
    • Bao, Y.1    Xie, H.2    Shan, J.3    Jiang, R.4    Zhang, Y.5    Guo, L.6    Zhang, R.7    Li, Y.8
  • 32
    • 0024523884 scopus 로고
    • The primary structure of Escherichia coli L-threonine dehydrogenase
    • B.D. Aronson, R.L. Somerville, B.R. Epperly, and E.E. Dekker The primary structure of Escherichia coli L-threonine dehydrogenase J. Biol. Chem. 264 1989 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
  • 33
    • 46849105863 scopus 로고    scopus 로고
    • Investigating a catalytic mechanism of hyperthermophilic L-threonine dehydrogenase from Pyrococcus horikoshii
    • N. Higashi, K. Tanimoto, M. Nishioka, K. Ishikawa, and M. Taya Investigating a catalytic mechanism of hyperthermophilic L-threonine dehydrogenase from Pyrococcus horikoshii J. Biochem. 144 2008 77 85
    • (2008) J. Biochem. , vol.144 , pp. 77-85
    • Higashi, N.1    Tanimoto, K.2    Nishioka, M.3    Ishikawa, K.4    Taya, M.5
  • 34
    • 70349453952 scopus 로고    scopus 로고
    • Structure and function of the L-threonine dehydrogenase (TkTHRDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
    • A. Bowyer, H. Mikolajek, J.W. Stuart, S.P. Wood, F. Jamil, N. Rashid, M. Akhtar, and J.B. Cooper Structure and function of the L-threonine dehydrogenase (TkTHRDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis J. Struct. Biol. 168 2009 294 304
    • (2009) J. Struct. Biol. , vol.168 , pp. 294-304
    • Bowyer, A.1    Mikolajek, H.2    Stuart, J.W.3    Wood, S.P.4    Jamil, F.5    Rashid, N.6    Akhtar, M.7    Cooper, J.B.8
  • 36
    • 17044438727 scopus 로고    scopus 로고
    • Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
    • N. Higashi, H. Fukada, and K. Ishikawa Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii J. Biosci. Bioeng. 99 2005 175 180
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 175-180
    • Higashi, N.1    Fukada, H.2    Ishikawa, K.3
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • H. Saito, and K. Miura Preparation of transforming deoxyribonucleic acid by phenol treatment Biochim. Biophys. Acta 72 1963 619 629
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 39
    • 58149133711 scopus 로고    scopus 로고
    • The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes
    • K.L. Kavanagh, H. Jörnvall, B. Persson, and U. Oppermann The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes Cell Mol. Life Sci. 65 2008 3895 3906
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jörnvall, H.2    Persson, B.3    Oppermann, U.4
  • 41
    • 29844441434 scopus 로고    scopus 로고
    • Structure and function of GDP-mannose-3',5'-epimerase: An enzyme which performs three chemical reactions at the same active site
    • L.L. Major, B.A. Wolucka, and J.H. Naismith Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site J. Am. Chem. Soc. 127 2005 18309 18320
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 18309-18320
    • Major, L.L.1    Wolucka, B.A.2    Naismith, J.H.3
  • 42
    • 0000364134 scopus 로고
    • The amino acid requirements of man. XI. The threonine and methionine requirements
    • W.C. Rose, M.J. Coon, H.B. Lockhart, and G.F. Lambert The amino acid requirements of man. XI. The threonine and methionine requirements J. Biol. Chem. 215 1955 101 110
    • (1955) J. Biol. Chem. , vol.215 , pp. 101-110
    • Rose, W.C.1    Coon, M.J.2    Lockhart, H.B.3    Lambert, G.F.4
  • 44
    • 46249096043 scopus 로고    scopus 로고
    • Luminal threonine concentration acutely affects intestinal mucosal protein and mucin synthesis in piglets
    • N.L. Nichols, and R.F. Bertolo Luminal threonine concentration acutely affects intestinal mucosal protein and mucin synthesis in piglets J. Nutr. 138 2008 1298 1303
    • (2008) J. Nutr. , vol.138 , pp. 1298-1303
    • Nichols, N.L.1    Bertolo, R.F.2
  • 46
    • 34249785691 scopus 로고    scopus 로고
    • A deficiency or excess of dietary threonine reduces protein synthesis in jejunum and skeletal muscle of young pigs
    • X. Wang, S. Qiao, Y. Yin, L. Yue, Z. Wang, and G. Wu A deficiency or excess of dietary threonine reduces protein synthesis in jejunum and skeletal muscle of young pigs J. Nutr. 137 2007 1442 1446
    • (2007) J. Nutr. , vol.137 , pp. 1442-1446
    • Wang, X.1    Qiao, S.2    Yin, Y.3    Yue, L.4    Wang, Z.5    Wu, G.6
  • 47
    • 77956651345 scopus 로고    scopus 로고
    • A moderate threonine deficiency affects gene expression profile, paracellular permeability and glucose absorption capacity in the ileum of piglets
    • A. Hamard, D. Mazurais, G. Boudry, I.L. Huërou-Luron, B. Sve, and N. Le Floc'h A moderate threonine deficiency affects gene expression profile, paracellular permeability and glucose absorption capacity in the ileum of piglets J. Nutr. Biochem. 21 2010 914 921
    • (2010) J. Nutr. Biochem. , vol.21 , pp. 914-921
    • Hamard, A.1    Mazurais, D.2    Boudry, G.3    Huërou-Luron, I.L.4    Sve, B.5    Le Floc'H, N.6
  • 48
    • 0014118812 scopus 로고
    • Concentrations of free glucogenic amino acids in livers of rats subjected to various metabolic stresses
    • D.H. Williamson, O. Lopes-vieira, and B. Walker Concentrations of free glucogenic amino acids in livers of rats subjected to various metabolic stresses Biochem. J. 104 1976 497 502
    • (1976) Biochem. J. , vol.104 , pp. 497-502
    • Williamson, D.H.1    Lopes-Vieira, O.2    Walker, B.3
  • 49
    • 0011195233 scopus 로고
    • L-threonine deaminase from thermophilic bacterium Bacillus stearothermophilus in ammonia sensor for L-threonine determination
    • T. Iida, S. Machida, N. Iijima, and T. Mitamura L-threonine deaminase from thermophilic bacterium Bacillus stearothermophilus in ammonia sensor for L-threonine determination Anal. Chem. Symp. Ser. 17 1983 631 636
    • (1983) Anal. Chem. Symp. Ser. , vol.17 , pp. 631-636
    • Iida, T.1    MacHida, S.2    Iijima, N.3    Mitamura, T.4
  • 50
    • 9744280392 scopus 로고    scopus 로고
    • Taxonomy of the genus Cupriavidus: A tale of lost and found
    • P. Vandamme, and T. Coenye Taxonomy of the genus Cupriavidus: a tale of lost and found Int. J. Syst. Evol. Microbiol. 54 2004 2285 2289
    • (2004) Int. J. Syst. Evol. Microbiol. , vol.54 , pp. 2285-2289
    • Vandamme, P.1    Coenye, T.2
  • 53
    • 0033813907 scopus 로고    scopus 로고
    • Kinetic analysis on inhibited growth and poly(3-hydroxybutyrate) formation of Alcaligenes eutrophus on acetate under nutrient-rich conditions
    • J. Wang, and J. Yu Kinetic analysis on inhibited growth and poly(3-hydroxybutyrate) formation of Alcaligenes eutrophus on acetate under nutrient-rich conditions Process Biochem. 36 2000 201 207
    • (2000) Process Biochem. , vol.36 , pp. 201-207
    • Wang, J.1    Yu, J.2
  • 54
    • 0035141753 scopus 로고    scopus 로고
    • Cleaner recovery of poly(3-hydroxybutyric acid) synthesized in Alcaligenes eutrophus
    • Y. Chen, H. Yang, Q. Zhou, J. Chen, and G. Gu Cleaner recovery of poly(3-hydroxybutyric acid) synthesized in Alcaligenes eutrophus Process Biochem. 36 2001 501 506
    • (2001) Process Biochem. , vol.36 , pp. 501-506
    • Chen, Y.1    Yang, H.2    Zhou, Q.3    Chen, J.4    Gu, G.5
  • 55
    • 77951719669 scopus 로고    scopus 로고
    • Classification of the short-chain dehydrogenase/reductase superfamily using hidden Markov models
    • Y. Kallberg, U. Oppermann, and B. Persson Classification of the short-chain dehydrogenase/reductase superfamily using hidden Markov models FEBS J. 277 2010 2375 2386
    • (2010) FEBS J. , vol.277 , pp. 2375-2386
    • Kallberg, Y.1    Oppermann, U.2    Persson, B.3
  • 57
    • 33947468266 scopus 로고
    • Rapid and specific determination of threonine
    • M. Flavin, and C. Slaughter Rapid and specific determination of threonine Anal. Chem. 31 1959 1983 1984
    • (1959) Anal. Chem. , vol.31 , pp. 1983-1984
    • Flavin, M.1    Slaughter, C.2


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