메뉴 건너뛰기




Volumn 273, Issue 12, 2006, Pages 2722-2729

Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus

Author keywords

Archaea; Hyperthermophile; Pyrococcus furiosus; Thermostability; Threonine dehydrogenase

Indexed keywords

ACETOIN; AMINO ACID DERIVATIVE; BACTERIAL ENZYME; CATION; COBALT; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SERINE; THREONINE 3 DEHYDROGENASE; UNCLASSIFIED DRUG; ZINC ION;

EID: 33745272829     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05290.x     Document Type: Article
Times cited : (20)

References (33)
  • 2
    • 0017196568 scopus 로고
    • Role of l-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli
    • Newman EB Kapoor V Potter R ( 1976) Role of l-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli. J Bacteriol 126, 1245 1249.
    • (1976) J Bacteriol , vol.126 , pp. 1245-1249
    • Newman, E.B.1    Kapoor, V.2    Potter, R.3
  • 3
    • 0017709111 scopus 로고
    • Role of threonine dehydrogenase in Escherichia coli threonine degradation
    • Potter R Kapoor V Newman EB ( 1977) Role of threonine dehydrogenase in Escherichia coli threonine degradation. J Bacteriol 132, 385 391.
    • (1977) J Bacteriol , vol.132 , pp. 385-391
    • Potter, R.1    Kapoor, V.2    Newman, E.B.3
  • 4
    • 0036375898 scopus 로고    scopus 로고
    • Medium-chain dehydrogenases/reductases (MDR): Family characterizations including genome comparisons and active site modelling
    • Nordling E Jornvall H Persson B ( 2002) Medium-chain dehydrogenases/ reductases (MDR): family characterizations including genome comparisons and active site modelling. Eur J Biochem 269, 4267 4276.
    • (2002) Eur J Biochem , vol.269 , pp. 4267-4276
    • Nordling, E.1    Jornvall, H.2    Persson, B.3
  • 6
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C Zeikus GJ ( 2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65, 1 43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 7
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • Fiala G Stetter KO ( 1986) Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch Microbiol 145, 56 61.
    • (1986) Arch Microbiol , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 8
    • 0028245448 scopus 로고
    • Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus
    • Kengen SWM De Bok FA Van Loo ND Dijkema C Stams AJM De Vos WM ( 1994) Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus. J Biol Chem 269, 17537 17541.
    • (1994) J Biol Chem , vol.269 , pp. 17537-17541
    • Kengen, S.W.M.1    De Bok, F.A.2    Van Loo, N.D.3    Dijkema, C.4    Stams, A.J.M.5    De Vos, W.M.6
  • 10
    • 0034826251 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Van der Oost J Voorhorst WG Kengen SWM Geerling ACM Wittenhorst V Gueguen Y DeVos WM ( 2001) Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur J Biochem 268, 3062 3068.
    • (2001) Eur J Biochem , vol.268 , pp. 3062-3068
    • Van Der Oost, J.1    Voorhorst, W.G.2    Kengen, S.W.M.3    Geerling, A.C.M.4    Wittenhorst, V.5    Gueguen, Y.6    Devos, W.M.7
  • 11
    • 0032988361 scopus 로고    scopus 로고
    • An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Ma K Adams MW ( 1999) An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 181, 1163 1170.
    • (1999) J Bacteriol , vol.181 , pp. 1163-1170
    • Ma, K.1    Adams, M.W.2
  • 12
    • 23944470849 scopus 로고    scopus 로고
    • L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: Gene cloning and enzymatic characterization
    • Shimizu Y Sakuraba H Kawakami R Goda S Kawarabayasi Y Ohshima T ( 2005) l-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: gene cloning and enzymatic characterization. Extremophiles 9, 317 324.
    • (2005) Extremophiles , vol.9 , pp. 317-324
    • Shimizu, Y.1    Sakuraba, H.2    Kawakami, R.3    Goda, S.4    Kawarabayasi, Y.5    Ohshima, T.6
  • 13
    • 17044438727 scopus 로고    scopus 로고
    • Kinetic study of thermostable l-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
    • Higashi N Fukada H Ishikawa K ( 2005) Kinetic study of thermostable l-threonine dehydrogenase from an archaeon Pyrococcus horikoshii. J Biosci Bioeng 99, 175 180.
    • (2005) J Biosci Bioeng , vol.99 , pp. 175-180
    • Higashi, N.1    Fukada, H.2    Ishikawa, K.3
  • 14
    • 33744469369 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of hyperthermophilic l-threonine dehydrogenase from the archaeon Pyrococcus horikoshii
    • Higashi N Matsuura T Nakagawa A Ishikawa K ( 2005) Crystallization and preliminary X-ray analysis of hyperthermophilic l-threonine dehydrogenase from the archaeon Pyrococcus horikoshii. Acta Crystallogr Sect F 61, 432 434.
    • (2005) Acta Crystallogr Sect F , vol.61 , pp. 432-434
    • Higashi, N.1    Matsuura, T.2    Nakagawa, A.3    Ishikawa, K.4
  • 15
    • 0019459723 scopus 로고
    • L-Threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12
    • Boylan SA Dekker EE ( 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
  • 16
    • 0024523884 scopus 로고
    • The primary structure of Escherichia colil-threonine dehydrogenase
    • Aronson BD Somerville RL Epperly BR Dekker EE ( 1989) The primary structure of Escherichia colil-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
  • 17
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga RK Terpstra P Hol WG ( 1986) Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol 187, 101 107.
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.3
  • 18
    • 0023411028 scopus 로고
    • Characteristics of alcohol/polyol dehydrogenases. the zinc-containing long-chain alcohol dehydrogenases
    • Jornvall H Persson B Jeffery J ( 1987) Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases. Eur J Biochem 167, 195 201.
    • (1987) Eur J Biochem , vol.167 , pp. 195-201
    • Jornvall, H.1    Persson, B.2    Jeffery, J.3
  • 19
    • 0026652564 scopus 로고
    • Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family
    • Sun HW Plapp BV ( 1992) Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family. J Mol Evol 34, 522 535.
    • (1992) J Mol Evol , vol.34 , pp. 522-535
    • Sun, H.W.1    Plapp, B.V.2
  • 20
    • 0028793102 scopus 로고
    • Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization
    • Chen YW Dekker EE Somerville RL ( 1995) Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization. Biochim Biophys Acta 1253, 208 214.
    • (1995) Biochim Biophys Acta , vol.1253 , pp. 208-214
    • Chen, Y.W.1    Dekker, E.E.2    Somerville, R.L.3
  • 21
    • 0032532659 scopus 로고    scopus 로고
    • Investigation of a catalytic zinc binding site in Escherichia colil-threonine dehydrogenase by site-directed mutagenesis of cysteine-38
    • Johnson AR Chen YW Dekker EE ( 1998) Investigation of a catalytic zinc binding site in Escherichia colil-threonine dehydrogenase by site-directed mutagenesis of cysteine-38. Arch Biochem Biophys 358, 211 221.
    • (1998) Arch Biochem Biophys , vol.358 , pp. 211-221
    • Johnson, A.R.1    Chen, Y.W.2    Dekker, E.E.3
  • 22
    • 0010394407 scopus 로고    scopus 로고
    • Structural characterization of the zinc site in Escherichia colil-threonine dehydrogenase using extended X-ray absorption fine structure spectroscopy
    • Clark-Baldwin K Johnson AR Chen YW Dekker EE Penner-Hahn JE ( 1998) Structural characterization of the zinc site in Escherichia colil-threonine dehydrogenase using extended X-ray absorption fine structure spectroscopy. Inorg Chim Acta 275-276, 215 221.
    • (1998) Inorg Chim Acta , vol.275-276 , pp. 215-221
    • Clark-Baldwin, K.1    Johnson, A.R.2    Chen, Y.W.3    Dekker, E.E.4    Penner-Hahn, J.E.5
  • 23
    • 0028853277 scopus 로고
    • Identification of a second active site residue in Escherichia colil-threonine dehydrogenase: Methylation of histidine-90 with methyl p-nitrobenzenesulfonate
    • Marcus JP Dekker EE ( 1995) Identification of a second active site residue in Escherichia colil-threonine dehydrogenase: methylation of histidine-90 with methyl p-nitrobenzenesulfonate. Arch Biochem Biophys 316, 413 420.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 413-420
    • Marcus, J.P.1    Dekker, E.E.2
  • 24
    • 0032029788 scopus 로고    scopus 로고
    • Site-directed mutagenesis of histidine-90 in Escherichia colil-threonine dehydrogenase alters its substrate specificity
    • Johnson AR Dekker EE ( 1998) Site-directed mutagenesis of histidine-90 in Escherichia colil-threonine dehydrogenase alters its substrate specificity. Arch Biochem Biophys 351, 8 16.
    • (1998) Arch Biochem Biophys , vol.351 , pp. 8-16
    • Johnson, A.R.1    Dekker, E.E.2
  • 25
    • 0025847512 scopus 로고
    • L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies
    • Epperly BR Dekker EE ( 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
  • 26
    • 0034934758 scopus 로고    scopus 로고
    • Characterization of hepatic l-threonine dehydrogenase of chicken
    • Yuan JH Austic RE ( 2001) Characterization of hepatic l-threonine dehydrogenase of chicken. Comp Biochem Physiol B Biochem Mol Biol 130, 65 73.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.130 , pp. 65-73
    • Yuan, J.H.1    Austic, R.E.2
  • 27
    • 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 ( 1986) Interaction between l-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production. J Biol Chem 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
  • 28
    • 0023277621 scopus 로고
    • Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli
    • Ravnikar PD Somerville RL ( 1987) Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli. J Bacteriol 169, 2611 2617.
    • (1987) J Bacteriol , vol.169 , pp. 2611-2617
    • Ravnikar, P.D.1    Somerville, R.L.2
  • 29
    • 0027363658 scopus 로고
    • Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme a lyase and threonine dehydrogenase
    • Marcus JP Dekker EE ( 1993) Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase. J Bacteriol 175, 6505 6511.
    • (1993) J Bacteriol , vol.175 , pp. 6505-6511
    • Marcus, J.P.1    Dekker, E.E.2
  • 31
    • 0037465682 scopus 로고    scopus 로고
    • Production of recombinant thermostable proteins expressed in Escherichia coli: Completion of protein synthesis is the bottleneck
    • Sorensen HP Sperling-Petersen HU Mortensen KK ( 2003) Production of recombinant thermostable proteins expressed in Escherichia coli: completion of protein synthesis is the bottleneck. J Chromatogr B Anal Technol Biomed Life Sci 786, 207 214.
    • (2003) J Chromatogr B Anal Technol Biomed Life Sci , vol.786 , pp. 207-214
    • Sorensen, H.P.1    Sperling-Petersen, H.U.2    Mortensen, K.K.3
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM ( 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.