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Volumn 96, Issue 3, 2007, Pages 559-569

One-pot synthesis of amino-alcohols using a de-novo transketolase and β-alanine:pyruvate transaminase pathway in Escherichia coli

Author keywords

Biocatalyst; Chiral amino alcohols; Transaminase; Transketolase

Indexed keywords

BIOCATALYSIS; CHIRAL AMINO-ALCOHOLS; ENZYMES TRANSKETOLASE (TK); PLASMIDS;

EID: 33846904594     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21125     Document Type: Article
Times cited : (129)

References (57)
  • 1
    • 0032883216 scopus 로고    scopus 로고
    • Metabolic engineering of the terpenoid biosynthesis pathway of Escherichia coli for production of carotenoids beta carotene and zeaxanthin
    • Albrecht M, Misawa N, Sandmann G. 1999. Metabolic engineering of the terpenoid biosynthesis pathway of Escherichia coli for production of carotenoids beta carotene and zeaxanthin. Biotechnol Lett 21:791-795.
    • (1999) Biotechnol Lett , vol.21 , pp. 791-795
    • Albrecht, M.1    Misawa, N.2    Sandmann, G.3
  • 2
    • 0033876920 scopus 로고    scopus 로고
    • Novel hydroxycarotenoids with imroved antioxidative properties produced by gene combination in Escherichia coli
    • Albrecht M, Takaichi S, Steiger S, Wang ZY, Sandmann G. 2000. Novel hydroxycarotenoids with imroved antioxidative properties produced by gene combination in Escherichia coli. Nat Biotechnol 18:843-846.
    • (2000) Nat Biotechnol , vol.18 , pp. 843-846
    • Albrecht, M.1    Takaichi, S.2    Steiger, S.3    Wang, Z.Y.4    Sandmann, G.5
  • 3
    • 0037008967 scopus 로고    scopus 로고
    • Deracemization of α-methylbenzylamine using an enzyme obtained by in vitro evolution
    • Alexeeva M, Enright A, Dawson MJ, Mahmoudian M, Turner NJ. 2002. Deracemization of α-methylbenzylamine using an enzyme obtained by in vitro evolution. Angew Chem Int Ed 41:3177-3180.
    • (2002) Angew Chem Int Ed , vol.41 , pp. 3177-3180
    • Alexeeva, M.1    Enright, A.2    Dawson, M.J.3    Mahmoudian, M.4    Turner, N.J.5
  • 4
    • 0034787233 scopus 로고    scopus 로고
    • Metabolic engineering of isoprenoids
    • Barkovich R, Liao JC. 2001. Metabolic engineering of isoprenoids. Met Eng 3:27-39.
    • (2001) Met Eng , vol.3 , pp. 27-39
    • Barkovich, R.1    Liao, J.C.2
  • 7
    • 0030448758 scopus 로고    scopus 로고
    • Carbon-carbon bond synthesis: Preparation and use of immobilised transketolase
    • Brocklebank S, Mitra RK, Woodley JM, Lilly MD. 1996. Carbon-carbon bond synthesis: Preparation and use of immobilised transketolase. Ann NY Acad Sci 799:729-736.
    • (1996) Ann NY Acad Sci , vol.799 , pp. 729-736
    • Brocklebank, S.1    Mitra, R.K.2    Woodley, J.M.3    Lilly, M.D.4
  • 8
    • 0032841351 scopus 로고    scopus 로고
    • Immobilised transketolase for carbon-carbon bond synthesis: Biocatalyst stability
    • Brocklebank S, Woodley JM, Lilly MD. 1999. Immobilised transketolase for carbon-carbon bond synthesis: Biocatalyst stability. J Mol Cat B - Enz 7:223-231.
    • (1999) J Mol Cat B - Enz , vol.7 , pp. 223-231
    • Brocklebank, S.1    Woodley, J.M.2    Lilly, M.D.3
  • 10
    • 0027305020 scopus 로고
    • Synthesis of a flourescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography
    • Cohon SA, Michaud DP. 1993. Synthesis of a flourescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography. Anal Biochem 211:279-287.
    • (1993) Anal Biochem , vol.211 , pp. 279-287
    • Cohon, S.A.1    Michaud, D.P.2
  • 11
    • 0029034026 scopus 로고
    • Diastereoselective conversion of L-(S)-Erythrulose to 2-amino-2-deoxy-L- erythritol
    • Dequeker E, Compernolle F, Toppet S, Hoornaert G. 1995. Diastereoselective conversion of L-(S)-Erythrulose to 2-amino-2-deoxy-L- erythritol. Tetrahedron 51:5877-5890.
    • (1995) Tetrahedron , vol.51 , pp. 5877-5890
    • Dequeker, E.1    Compernolle, F.2    Toppet, S.3    Hoornaert, G.4
  • 12
    • 0035794308 scopus 로고    scopus 로고
    • Porcine pancreatic lipase mediated regio- and stereoselective hydrolysis: Chemoenzymatic synthesis of (2S,3S)-2-amino-3,4-dihydroxybutyric acid
    • Fadnavis NW, Sharfuddin M, Kumara Vadivel S. 2001. Porcine pancreatic lipase mediated regio- and stereoselective hydrolysis: Chemoenzymatic synthesis of (2S,3S)-2-amino-3,4-dihydroxybutyric acid. Tetrahedron: Asymm 12:691-693.
    • (2001) Tetrahedron: Asymm , vol.12 , pp. 691-693
    • Fadnavis, N.W.1    Sharfuddin, M.2    Kumara Vadivel, S.3
  • 13
    • 0032861512 scopus 로고    scopus 로고
    • Engineering of a novel biochemical pathway for the biosynthesis of L-2-aminobutyric Acid in Escherichia coli K12
    • Fotheringham G, Grinter N, Pantaleone DP, Senkpeil RF. 1999. Engineering of a novel biochemical pathway for the biosynthesis of L-2-aminobutyric Acid in Escherichia coli K12. Bioorgan Med Chem 7:2209-2213.
    • (1999) Bioorgan Med Chem , vol.7 , pp. 2209-2213
    • Fotheringham, G.1    Grinter, N.2    Pantaleone, D.P.3    Senkpeil, R.F.4
  • 14
    • 0031081566 scopus 로고    scopus 로고
    • Kinetics of overexpressed transketolase from E.coli JM107/pQR 700
    • Gyamerah M, Willetts AJ. 1997. Kinetics of overexpressed transketolase from E.coli JM107/pQR 700. Enz Microb Tech 20:127-134.
    • (1997) Enz Microb Tech , vol.20 , pp. 127-134
    • Gyamerah, M.1    Willetts, A.J.2
  • 16
    • 0029931442 scopus 로고    scopus 로고
    • Enzymatic synthesis of 'natural-labelled' 6-Deoxy-L-Sorbose precursor of an important food flavour
    • Hecquet L, Bolte J, Demuynck C. 1996. Enzymatic synthesis of 'natural-labelled' 6-Deoxy-L-Sorbose precursor of an important food flavour. Tetrahedron 52:8223-8232.
    • (1996) Tetrahedron , vol.52 , pp. 8223-8232
    • Hecquet, L.1    Bolte, J.2    Demuynck, C.3
  • 18
    • 0343182984 scopus 로고    scopus 로고
    • Enzyme catalyzed carbon-carbon bond formation: Large scale production of Escherichia coli transketolase
    • Hobbs GR, Mitra RK, Chauhan RP, Woodley JM, Lilly MD. 1996. Enzyme catalyzed carbon-carbon bond formation: large scale production of Escherichia coli transketolase. J Biotechnol 45:173-179.
    • (1996) J Biotechnol , vol.45 , pp. 173-179
    • Hobbs, G.R.1    Mitra, R.K.2    Chauhan, R.P.3    Woodley, J.M.4    Lilly, M.D.5
  • 19
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine-residues
    • Hochuli E, Dobeli H, Schacher A. 1987. New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine-residues. J Chromatogr 411:177-184.
    • (1987) J Chromatogr , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 20
    • 0038735348 scopus 로고    scopus 로고
    • Ferredoxin reductase enhances heterologously expressed cytochrome CYP105D1 in Escherichia coli and streptomyces lividans
    • Hussain HA, Ward JM, 2003. Ferredoxin reductase enhances heterologously expressed cytochrome CYP105D1 in Escherichia coli and streptomyces lividans. Enzyme Microb Technol 32:790-800.
    • (2003) Enzyme Microb Technol , vol.32 , pp. 790-800
    • Hussain, H.A.1    Ward, J.M.2
  • 21
    • 0033009718 scopus 로고    scopus 로고
    • Hyperproduction of tryptophan by Corynebacterium glutamicum with the modified pentose phosphate Pathway
    • Ikeda M, Katsumata R. 1999. Hyperproduction of tryptophan by Corynebacterium glutamicum with the modified pentose phosphate Pathway. Appl Environ Microbiol 65:2497-2502.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2497-2502
    • Ikeda, M.1    Katsumata, R.2
  • 22
    • 33846920826 scopus 로고    scopus 로고
    • Ingram CU, 2006. Biocatalytic synthesis of amino-alcohols using a de novo designed transketolase-β-alanine: pyruvate transaminase pathway in Escherichia coli. PhD thesis University of London (University College).
    • Ingram CU, 2006. Biocatalytic synthesis of amino-alcohols using a de novo designed transketolase-β-alanine: pyruvate transaminase pathway in Escherichia coli. PhD thesis University of London (University College).
  • 24
    • 2942720171 scopus 로고
    • Purification and properties of amine alpha-ketogluterate transaminase from Escherichia coli
    • Kim K-H. 1964. Purification and properties of amine alpha-ketogluterate transaminase from Escherichia coli. J Biol Chem 239:783-786.
    • (1964) J Biol Chem , vol.239 , pp. 783-786
    • Kim, K.-H.1
  • 25
    • 0035916370 scopus 로고    scopus 로고
    • Metabolic engineering of the nonmevalonate isopentenyl diphosphate synthasis pathway in Escherichia coli enhance lycopene production
    • Kim SW, Keasling JD. 2001. Metabolic engineering of the nonmevalonate isopentenyl diphosphate synthasis pathway in Escherichia coli enhance lycopene production. Biotechnol Bioeng 72:408-415.
    • (2001) Biotechnol Bioeng , vol.72 , pp. 408-415
    • Kim, S.W.1    Keasling, J.D.2
  • 26
    • 0035812794 scopus 로고    scopus 로고
    • Orthagonally protected enatiopure syn-2-amino-1,3,4-butanetrols: A general building block for syn-amino alcohols
    • Kwon SJ, Ko SY. 2001. Orthagonally protected enatiopure syn-2-amino-1,3,4-butanetrols: A general building block for syn-amino alcohols. J Org Chem 66:6833-6835.
    • (2001) J Org Chem , vol.66 , pp. 6833-6835
    • Kwon, S.J.1    Ko, S.Y.2
  • 27
    • 0037148017 scopus 로고    scopus 로고
    • Synthesis of statine employing a general syn-amino alcohol building block
    • Kwon SJ, Ko SY. 2002. Synthesis of statine employing a general syn-amino alcohol building block. Tetrahedron: Lett 43:639-641.
    • (2002) Tetrahedron: Lett , vol.43 , pp. 639-641
    • Kwon, S.J.1    Ko, S.Y.2
  • 28
    • 4544320177 scopus 로고    scopus 로고
    • Fermentative production of L-cysteine with a recombinant Escherichia coli strain
    • Maier T, Winterhalter C. 2000. Fermentative production of L-cysteine with a recombinant Escherichia coli strain. Chem Abstracts 133:361976.
    • (2000) Chem Abstracts , vol.133 , pp. 361976
    • Maier, T.1    Winterhalter, C.2
  • 30
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta P, Hale TI, Christen P. 1993. Aminotransferases: Demonstration of homology and division into evolutionary subgroups. Eur J Biochem 214:549-561.
    • (1993) Eur J Biochem , vol.214 , pp. 549-561
    • Mehta, P.1    Hale, T.I.2    Christen, P.3
  • 31
    • 0037074092 scopus 로고    scopus 로고
    • Efficient synthesis of (2R,3S)-and (2S,3S)-2-amino-1,3,4-butanetriols through stereodivergent hydroxymethylation of D-glyceraldehyde nitrones
    • Merino P, Fransco S, Merchan FL, Revuelta J, Tejero T. 2002. Efficient synthesis of (2R,3S)-and (2S,3S)-2-amino-1,3,4-butanetriols through stereodivergent hydroxymethylation of D-glyceraldehyde nitrones. Tetrahedron Lett 43:459-462.
    • (2002) Tetrahedron Lett , vol.43 , pp. 459-462
    • Merino, P.1    Fransco, S.2    Merchan, F.L.3    Revuelta, J.4    Tejero, T.5
  • 32
    • 0025630190 scopus 로고
    • Elucidation of the Erwinia uredovora carotenoid biosynthelic pathway by functional analysis of gene products expressed in Escherichia coli
    • Misawa N, Nakagawa M, Kobayashi K, Yamano S, Izawa Y, Nakamura K, Harashima K. 1990. Elucidation of the Erwinia uredovora carotenoid biosynthelic pathway by functional analysis of gene products expressed in Escherichia coli. J Bacteriol 172:6704-6712.
    • (1990) J Bacteriol , vol.172 , pp. 6704-6712
    • Misawa, N.1    Nakagawa, M.2    Kobayashi, K.3    Yamano, S.4    Izawa, Y.5    Nakamura, K.6    Harashima, K.7
  • 33
    • 0030024493 scopus 로고    scopus 로고
    • A useful assay for transketolase in asymmetric synthesis
    • Mitra RK, Woodley JM. 1996. A useful assay for transketolase in asymmetric synthesis. Biotechnol Tech 10:167-172.
    • (1996) Biotechnol Tech , vol.10 , pp. 167-172
    • Mitra, R.K.1    Woodley, J.M.2
  • 34
    • 0031973750 scopus 로고    scopus 로고
    • Mitra RK, Woodley JM, Lilly MD. 1998. E. coli transketolase- catalyzed carbon-carbon bond formation:Biotransformation characterization for reactor evaluation and selection. Enzyme Microb Technol 22:64-70.
    • Mitra RK, Woodley JM, Lilly MD. 1998. E. coli transketolase- catalyzed carbon-carbon bond formation:Biotransformation characterization for reactor evaluation and selection. Enzyme Microb Technol 22:64-70.
  • 35
    • 0033618633 scopus 로고    scopus 로고
    • A stereo synthesis of (-)detoxinine from L-ascorbic acid
    • Monache GD, Misiti D, Zappia G. 1999. A stereo synthesis of (-)detoxinine from L-ascorbic acid. Tetrahedron: Asymm 10:2961-2973.
    • (1999) Tetrahedron: Asymm , vol.10 , pp. 2961-2973
    • Monache, G.D.1    Misiti, D.2    Zappia, G.3
  • 36
    • 0018393210 scopus 로고
    • Preliminary crystallographic study of w-aminotransferase from Pseudomonas sp. F-126
    • Morita Y, Aibara S, Yonaha K, Soda K. 1979. Preliminary crystallographic study of w-aminotransferase from Pseudomonas sp. F-126. J Mol Biol 130:211-213.
    • (1979) J Mol Biol , vol.130 , pp. 211-213
    • Morita, Y.1    Aibara, S.2    Yonaha, K.3    Soda, K.4
  • 37
    • 0003594801 scopus 로고
    • R)- and (S)-2,3-isopropylidene glyceraldehyde-'unbiased' chiral strating materials
    • Mulzer J, Waldmann H, editors, New York: Wiley. p
    • Mulzer J. 1991. (R)- and (S)-2,3-isopropylidene glyceraldehyde-'unbiased' chiral strating materials. In: Mulzer J, Waldmann H, editors. Organ Synth Highlights. New York: Wiley. p 243-250.
    • (1991) Organ Synth Highlights , pp. 243-250
    • Mulzer, J.1
  • 38
    • 3543087310 scopus 로고    scopus 로고
    • Trends and innovation in industrial biocatalysis for the production of fine chemicals
    • Panke S, Held M, Wubbolts M. 2004. Trends and innovation in industrial biocatalysis for the production of fine chemicals. Curr Opin Biotech 15:272-279.
    • (2004) Curr Opin Biotech , vol.15 , pp. 272-279
    • Panke, S.1    Held, M.2    Wubbolts, M.3
  • 39
    • 0037199154 scopus 로고    scopus 로고
    • Modeling and kinetic analysis of the reaction system using whole cells with separately and co-expressed D-hydantoinase and N-carbamoylase
    • Park JH, Oh KH, Lee DC, Kim HS. 2002. Modeling and kinetic analysis of the reaction system using whole cells with separately and co-expressed D-hydantoinase and N-carbamoylase. Biotechnol Bioeng 78:779-793.
    • (2002) Biotechnol Bioeng , vol.78 , pp. 779-793
    • Park, J.H.1    Oh, K.H.2    Lee, D.C.3    Kim, H.S.4
  • 40
    • 0033213706 scopus 로고    scopus 로고
    • The discovery of a mevalonate independent pathway for isoprenoid biosynthesis in bacteria and higher plants
    • Rohmer M. 1999. The discovery of a mevalonate independent pathway for isoprenoid biosynthesis in bacteria and higher plants. Nat Prod Rep 16:565-574.
    • (1999) Nat Prod Rep , vol.16 , pp. 565-574
    • Rohmer, M.1
  • 41
    • 0033941389 scopus 로고    scopus 로고
    • Molecular breeding of carotenoid biosynthetic pathways
    • Schmidt-Dannert C, Umeno D, Arnold FH. 2000. Molecular breeding of carotenoid biosynthetic pathways. Nat Biotechnol 18:750-753.
    • (2000) Nat Biotechnol , vol.18 , pp. 750-753
    • Schmidt-Dannert, C.1    Umeno, D.2    Arnold, F.H.3
  • 42
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the mythsbiocatalysis in industrial synthesis
    • Schoemaker HE, Mink D, Wubbolts MG. 2003. Dispelling the mythsbiocatalysis in industrial synthesis. Science 299:1694-1697.
    • (2003) Science , vol.299 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    Wubbolts, M.G.3
  • 43
    • 0035433593 scopus 로고    scopus 로고
    • Comparison of the omega transaminases from different microorganisms and application to production of chiral amines
    • Shin J-S, Kim B-G. 2001. Comparison of the omega transaminases from different microorganisms and application to production of chiral amines. Biosci Biotechnol Biochem 65:1782-1788.
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 1782-1788
    • Shin, J.-S.1    Kim, B.-G.2
  • 44
    • 0037012917 scopus 로고    scopus 로고
    • Exploring the active site of amine:pyruvate aminotransferase on the basis of the substrate structure-reactivity relationship: How the enzyme controls substrate specificity and stereoselectivity
    • Shin J-S, Kim B-G. 2002. Exploring the active site of amine:pyruvate aminotransferase on the basis of the substrate structure-reactivity relationship: How the enzyme controls substrate specificity and stereoselectivity. J Org Chem 67:2848-2853.
    • (2002) J Org Chem , vol.67 , pp. 2848-2853
    • Shin, J.-S.1    Kim, B.-G.2
  • 45
    • 0038236890 scopus 로고    scopus 로고
    • Shin J-S, Yun H, Jang J-W, Park I, Kim B-G. 2003. Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17. Appl Microbiol Biotechnol 61:463-471.
    • Shin J-S, Yun H, Jang J-W, Park I, Kim B-G. 2003. Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17. Appl Microbiol Biotechnol 61:463-471.
  • 46
    • 0000980630 scopus 로고
    • The use of aminotransferases for the production of chiral amino acids and amines
    • Collins AN, Sheldrake GN, Crosby J, editors, New York: Wiley & sons Ltd. pp
    • Stirling DI. 1992. The use of aminotransferases for the production of chiral amino acids and amines. In: Collins AN, Sheldrake GN, Crosby J, editors. Chirality in industry. New York: Wiley & sons Ltd. pp 209-222.
    • (1992) Chirality in industry , pp. 209-222
    • Stirling, D.I.1
  • 47
    • 0036900263 scopus 로고    scopus 로고
    • The production of fine chemicals by biotransformation
    • Straathof AJJ, Panke S, Schmid A. 2002. The production of fine chemicals by biotransformation. Curr Opin Biotech 13:548-556.
    • (2002) Curr Opin Biotech , vol.13 , pp. 548-556
    • Straathof, A.J.J.1    Panke, S.2    Schmid, A.3
  • 48
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier WF, Moffatt BA. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, W.F.1    Moffatt, B.A.2
  • 49
    • 0033585443 scopus 로고    scopus 로고
    • Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli
    • Wang CW, Oh MK, Liao JC. 1999. Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli. Biotechnol Bioeng 62:235-241.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 235-241
    • Wang, C.W.1    Oh, M.K.2    Liao, J.C.3
  • 50
    • 20244378184 scopus 로고
    • Crystal structure analysis of w-amino acid:pyruvate aminotransferase with newly developed weissenberg camera and an imaging plate using synchrotron radiation
    • Watanabe N, Sakabe K, Sakabe N, Higashi T, Sasaki K, Aibara S, Morita Y, Yonoha K, Toyama S, Fukutani H. 1989. Crystal structure analysis of w-amino acid:pyruvate aminotransferase with newly developed weissenberg camera and an imaging plate using synchrotron radiation. J Biochem 105:1-3.
    • (1989) J Biochem , vol.105 , pp. 1-3
    • Watanabe, N.1    Sakabe, K.2    Sakabe, N.3    Higashi, T.4    Sasaki, K.5    Aibara, S.6    Morita, Y.7    Yonoha, K.8    Toyama, S.9    Fukutani, H.10
  • 51
    • 4644241379 scopus 로고    scopus 로고
    • Challenges in the development of an efficient enzymatic process in the pharmaceutical industry
    • Yazbeck DR, Martinez CA, Hu S, Tao J. 2004. Challenges in the development of an efficient enzymatic process in the pharmaceutical industry. Tetrahedron: Asymm 15:2757-2763.
    • (2004) Tetrahedron: Asymm , vol.15 , pp. 2757-2763
    • Yazbeck, D.R.1    Martinez, C.A.2    Hu, S.3    Tao, J.4
  • 52
    • 0017094068 scopus 로고
    • Purification and crystallisation of bacterial w-aminoacid-pyruvate aminotransferase
    • Yonaha K, Toyama M, Yasuda M, Soda K. 1976. Purification and crystallisation of bacterial w-aminoacid-pyruvate aminotransferase. FEBS Lett 71:21-24.
    • (1976) FEBS Lett , vol.71 , pp. 21-24
    • Yonaha, K.1    Toyama, M.2    Yasuda, M.3    Soda, K.4
  • 53
    • 0021111654 scopus 로고
    • Properties of the Bound Coenzyme and Subunit Structure of w-AminoAcid:Pyruvate Amino-transferase
    • Yonaha K, Toyama M, Kagamiyama H. 1983. Properties of the Bound Coenzyme and Subunit Structure of w-AminoAcid:Pyruvate Amino-transferase. J Biol Chem 258:2260-2265.
    • (1983) J Biol Chem , vol.258 , pp. 2260-2265
    • Yonaha, K.1    Toyama, M.2    Kagamiyama, H.3
  • 54
    • 0026747089 scopus 로고
    • The primary structure of ω-aminoacid:pyruvate aminotransferase
    • Yonaha K, Nishie M, Aibara S. 1992. The primary structure of ω-aminoacid:pyruvate aminotransferase. J Biol Chem 267:12506-12510.
    • (1992) J Biol Chem , vol.267 , pp. 12506-12510
    • Yonaha, K.1    Nishie, M.2    Aibara, S.3
  • 55
    • 0017751923 scopus 로고    scopus 로고
    • Properties of Crystalline omega-Amino Acid:Pyruvate Aminotransferase of Pseudomonas sp. F-126
    • Yonaha K, Toyama S, Yasuda M, Soda K, 1997. Properties of Crystalline omega-Amino Acid:Pyruvate Aminotransferase of Pseudomonas sp. F-126. Agri Biol Chem 41:1701-1706.
    • (1997) Agri Biol Chem , vol.41 , pp. 1701-1706
    • Yonaha, K.1    Toyama, S.2    Yasuda, M.3    Soda, K.4
  • 56
    • 33645557831 scopus 로고    scopus 로고
    • Synthesis of enantiomerically pure trans-(1R,2R)- and cis-(1S,2R)-1-amino-2-indanol by lipase and ω-transaminase
    • Yun H, Kim J, Kinnera K, Kim B-G. 2006. Synthesis of enantiomerically pure trans-(1R,2R)- and cis-(1S,2R)-1-amino-2-indanol by lipase and ω-transaminase. Biotech Bioeng 93(2):391-395.
    • (2006) Biotech Bioeng , vol.93 , Issue.2 , pp. 391-395
    • Yun, H.1    Kim, J.2    Kinnera, K.3    Kim, B.-G.4


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