IP Library › Granted Patent US 12,448,611
Granted Patent B2
US 12,448,611 · App. 18/409,699 · Granted Oct 21, 2025

Transaminase polypeptides

Inventors: Ish K. Dhawan (Foster City, CA); Gregory Miller (Redwood City, CA); Xiyun Zhang (Fremont, CA)
Assignee: Codexis, Inc.
C12N9/1096C12P13/001C12P41/006C12Y206/01C12Y206/01018Y02P20/52
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,448,611
App. No.
18/409,699
Filed
Jan 10, 2024
Granted
Oct 21, 2025
Kind
B2
Art Unit
1652
USPC
435/193
Abstract

The present disclosure provides engineered transaminase enzymes having improved properties as compared to a naturally occurring wild-type transaminase enzyme. Also provided are polynucleotides encoding the engineered transaminase enzymes, host cells capable of expressing the engineered transaminase enzymes, and methods of using the engineered transaminase enzymes to synthesize a variety of chiral compounds.

Claims (20)

1. An engineered transaminase polypeptide, wherein said transaminase polypeptide comprises a polypeptide sequence at least 90% identical to SEQ ID NO: 2, wherein the transaminase polypeptide comprises a substitution selected from the group consisting of X294 is V, X324 is G, and X391 is A, and wherein the transaminase polypeptide has increased transaminase activity as compared to SEQ ID NO: 2 for conversion of an amino acceptor substrate to the corresponding chiral amino product.

2. The engineered transaminase polypeptide of claim 1 , wherein said polypeptide has at least 10% residual activity in the conversion of pyruvate to L-alanine in the presence of amino donor isopropylamine after treatment of the polypeptide at 50° C. for 23 h.

3. The engineered transaminase polypeptide of claim 1 , wherein the transaminase polypeptide sequence further comprises at least one additional substitution at a residue position selected from the group consisting of: X9, X21, X45, X86, X177, X208, and X211.

4. The engineered transaminase polypeptide of claim 3 , wherein the at least one additional substitution is selected from the group consisting of: X9 is T; X21 is N; X45 is H; X86 is A, G, H, N, S, Y; X177 is L; X208 is I; and X211 is K.

5. The engineered transaminase polypeptide of claim 1 , wherein the transaminase polypeptide sequence further comprises at least one substitution selected from the group consisting of: X30 is A; X31 is A; X44 is A; X56 is V; X57 is, A, C, F, I, L, or S; X81 is D; X82 is H; X85 is A, C, S, N, T, G, or V; X95 is T; X112 is I; X113 is C or H; X127 is L; X147 is G; X153 is A, C, G, N, M, Q, S, or T; X166 is S; X181 is R; X208 is I; X228 is G or T; X233 is L, S, I, V, N, G, or T; V297 is A, S, T, I, M, Q, C, or G; X311 is V; X314 is T or V; X317 is L, M, or Y; X318 is G, F, C, K, W, or R; X319 is Q, G, M, N, or V, X320 is A or K; X321 is L, M, or I; X385 is R; X398 is R; X407 is S; X408 is A; X409 is G; X415 is M; X417 is A, C, E, F, I, N, Q, Y, S, T, or V; X420 is N; X434 is V; and X438 is L.

6. The engineered transaminase polypeptide of claim 1 , wherein the transaminase polypeptide sequence further comprises at least one substitution set selected from the group consisting of: X12 is G and X434 is V; X44 is A and X166 is S; X57 is I and X153 is S; X81 is D and X86 is H; X82 is H and X417 is F; X85 is A and X317 is L; X85 is S and X153 is A; X85 is A and X153 is A; X85 is S and X153 is S; X86 is S and X153 is S; X86 is H and X153 is A; X112 is I and X317 is L; X113 is H and X407 is S; X153 is S and X233 is S; X311 is V and X314 is T; X314 is V and X409 is G; and X318 is G and X408 is A.

7. The engineered transaminase polypeptide of claim 1 , wherein the transaminase polypeptide sequence further comprises at least one substitution set selected from the group consisting of: X57 is A, X153 is S and X318 is G; X57 is F, X86 is H and X153 is Q; X57 is I, X86 is F and X320 is A; X57 is F, X86 is F and X153 is Q; X57 is A, X153 is C and X321 is L; X57 is C, X86 is S and X417 is T; X57 is C, X86 is A and X317 is L; X57 is F, X318 is F and X417 is S; X57 is L, X86 is S and X153 is A; X57 is F, X318 is G and X417 is I, X57 is L, X86 is F and X318 is F; X57 is L, X417 is C and X438 is L; X57 is F, X127 is L and X417 is C; X57 is S, X233 is L and X417 is V; X57 is S, X86 is G and X417 is C; X85 is A, X147 is G and X153 is A; X85 is S, X153 is A and X233 is T; X85 is A, X153 is S and X417 is S; X86 is H, X153 is A and X417 is C; X86 is H, X153 is S and X417 is C; X86 is F, X153 is C and X297 is A; X86 is S, X153 is T and X297 is A; X86 is H, X233 is L and X417 is A; X86 is F, X318 is R and X417 is A; X86 is N, X228 is G and X317 is L; X95 is T, X153 is A and X417 is C; X113 is C, X385 is R and X417 is C; X153 is A, X317 is L and X318 is G; X153 is A, X233 is T and X417 is C; X153 is S, X318 is R and X417 is E; X153 is C, X233 is L and X318 is R; X153 is T, X228 is G and X321 is L; X153 is S, X317 is L and X417 is C; X153 is T, X319 is V and X417 is I; X153 is S, X228 is G and X417 is V; X153 is C, X317 is Y and X319 is Q; X153 is T, X228 is G and X417 is A; X228 is G, X317 is L and X417 is C; X228 is G, X318 is G and X417 is C; X233 is L, X321 is L and X417 is I; and X317 is L, X318 is R and X417 is T.

8. The engineered transaminase polypeptide of claim 1 , wherein the transaminase polypeptide sequence further comprises at least one of the following substitution sets:

X57 is L and X86 is F and X153 is S and X233 is T and X417 is T;

X86 is H and X153 is A and XA228 is G and X417 is I; and

X86 is H and X153 is S and X181 is R and X417 is T.

9. The engineered transaminase polypeptide of claim 1 , wherein the polypeptide sequence that is at least 90% identical to SEQ ID NO: 2 and comprises the substitution is selected from the group consisting of SEQ ID NO: 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106, 108, 110, 112, 114, 116, 118, 120, 122, 124, 126, 128, 130, 132, 134, 136, 138, 140, 142, 144, 146, 148, 150, 152, 154, 156, 158, 160, 162, 164, 166, 168, 170, 172, 174, 176, 178, 180, 182, 184, 186, 188, 190, and 192.

10. The engineered transaminase polypeptide of claim 1 , wherein the transaminase polypeptide converts the amino acceptor substrate to the corresponding amino product with improved R-enantioselectivity as compared to a polypeptide set forth in SEQ ID NO: 18.

11. The engineered transaminase polypeptide of claim 10 , wherein the transaminase polypeptide sequence further comprises at least one substitution selected from the group consisting of: X57 is L, X81 is D, X82 is H, X85 is A, C, N, T, or V; X95 is T; X112 is I; X147 is G; X153 is A, S, N, G, or T; X233 is S or T; X317 is L, X318 is G or R; and X319 is V.

12. The engineered transaminase polypeptide of claim 10 , wherein the transaminase polypeptide sequence further comprises at least one substitution or substitution set selected from the group consisting of: X85 is A; X85 is A and X153 is A; and X85 is S and X153 is A.

13. The engineered transaminase polypeptide of claim 10 , wherein the transaminase polypeptide sequence is selected from the group consisting of SEQ ID NO: 22, 30, 32, 34, 36, 40, 44, 48, 56, 58, 60, 62, 64, 66, 68, 70, 72, 76, 84, 88, 90, 92, 104, 108, 110, 120, 122, 124, 126, 128, 132, 160, and 176.

14. The engineered transaminase polypeptide of claim 1 , wherein the transaminase enzyme polypeptide converts an amino acceptor substrate selected from 3,4-dihydronaphthalen-1 (2H)-one, 1-phenylbutan-2-one, 3,3-dimethylbutan-2-one, octan-2-one, ethyl 3-oxobutanoate, 4-phenylbutan-2-one, and 1-(4-bromophenyl) ethanone to the corresponding amine product at a rate that is greater than a polypeptide set forth in SEQ ID NO: 18.

15. The engineered transaminase polypeptide of claim 14 , wherein the transaminase polypeptide sequence comprises at least one additional substitution or substitution set selected from the group consisting of: X30 is A; X31 is A; X57 is I; X82 is H; X85 is V; X85 is C; X153 is S; X177 is L; X317 is M; X317 is Y; X417 is A; X319 is Q; X320 is A; X417 is I; X113 is H and X407 is S; X44 is A and X166 is S; X314 is V and X409 is G; X153 is S and X233 is S; X311 is V and X314 is T; X153 is S, X318 is R and X417 is E; X153 is C, X233 is L and X318 is R; X153 is S, X317 is L and X417 is C; X233 is L, X321 is L, and X417 is I; and X153 is C, X317 is Y and X319 is Q.

16. The engineered transaminase polypeptide of claim 14 , wherein the transaminase polypeptide sequence is selected from the group consisting of SEQ ID NO: 38, 42, 44, 52, 56, 66, 74, 76, 78, 80, 82, 84, 94, 96, 98, 100, 104, 118, 160, 164, 172, 184, and 188.

17. The engineered transaminase polypeptide of claim 14 , wherein the transaminase polypeptide converts the amino acceptor substrate 1-phenylbutan-2-one to the amino product(S)-1-phenylbutan-2-amine with improved S-enantioselectivity as compared to SEQ ID NO: 18.

Assignments (1)
SECURITY INTEREST Recorded Feb 15, 2024
From: CODEXIS, INC.
To: INNOVATUS LIFE SCIENCES LENDING FUND I, LP, AS COLLATERAL AGENT
Reel/Frame 066600/0650 →
Continuity (12)
Continuation 18060517 · Nov 30, 2022
Continuation 17224008 · Apr 6, 2021
Continuation 16717596 · Dec 17, 2019
Continuation 16399488 · Apr 30, 2019
Continuation 16018247 · Jun 26, 2018
Continuation 15912892 · Mar 6, 2018
Continuation 15341631 · Nov 2, 2016
Division 14684916 · Apr 13, 2015
Division 13920902 · Jun 18, 2013
Continuation 12684864 · Jan 8, 2010
Provisional Application 61143401 · Jan 8, 2009
Related Publication 20240150732A1 · May 9, 2024
References Cited (126)
US 4518692A · Rozzell · 1985 [cited by applicant]
US 4826766A · Rozzell · 1989 [cited by applicant]
US 4950606A · Stirling et al. · 1990 [cited by applicant]
US 5169780A · Stirling et al. · 1992 [cited by applicant]
US 5300437A · Stirling et al. · 1994 [cited by applicant]
US 5316943A · Kidman et al. · 1994 [cited by applicant]
US 5346828A · Stirling et al. · 1994 [cited by applicant]
US 5360724A · Matcham et al. · 1994 [cited by applicant]
US 5814473A · Patrick et al. · 1998 [cited by applicant]
US 5866512A · Matcham et al. · 1999 [cited by applicant]
US 5965432A · Kobayashi et al. · 1999 [cited by applicant]
US 6107521A · Lin et al. · 2000 [cited by applicant]
US 6133018A · Wu et al. · 2000 [cited by applicant]
US 6197558B1 · Fotheringham · 2001 [cited by applicant]
US 6221638B1 · Yamada et al. · 2001 [cited by applicant]
US 6344351B2 · Yamada et al. · 2002 [cited by applicant]
US 6346402B1 · Iwasaki et al. · 2002 [cited by applicant]
US 6413752B1 · Takashima et al. · 2002 [cited by applicant]
US 6727083B2 · Takashima et al. · 2004 [cited by applicant]
US 7169592B2 · Yamada et al. · 2007 [cited by applicant]
US 7172885B2 · Pannuri et al. · 2007 [cited by applicant]
US 7267969B2 · Pannuri et al. · 2007 [cited by applicant]
US 7276360B2 · Pannuri et al. · 2007 [cited by applicant]
US 8470564B2 · Dhawan et al. · 2013 [cited by applicant]
US 9029106B2 · Dhawan et al. · 2015 [cited by applicant]
US 9512410B2 · Dhawan et al. · 2016 [cited by applicant]
US 9617573B2 · Quintanar-Audelo · 2017 [cited by examiner]
US 9944909B2 · Dhawan et al. · 2018 [cited by applicant]
US 10196657B2 · Pearlman et al. · 2019 [cited by applicant]
US 10323233B2 · Dhawan et al. · 2019 [cited by applicant]
US 10323234B2 · Dhawan et al. · 2019 [cited by applicant]
US 10550370B2 · Dhawan et al. · 2020 [cited by applicant]
US 10995323B2 · Dhawan et al. · 2021 [cited by applicant]
US 11542485B2 · Dhawan et al. · 2023 [cited by applicant]
US 11939602B2 · Dhawan · 2024 [cited by examiner]
US 20070259410A1 · Donaldson et al. · 2007 [cited by applicant]
US 20080213845A1 · Fotheringham et al. · 2008 [cited by applicant]
US 20090117627A1 · Doderer et al. · 2009 [cited by applicant]
US 20140115737A1 · Abad · 2014 [cited by applicant]
US 20160024540A1 · Debarge et al. · 2016 [cited by applicant]
US 20210230564A1 · Dhawan et al. · 2021 [cited by applicant]
EP 1075534A1 · 2001 [cited by applicant]
JP 63273486A · 1988 [cited by applicant]
KR 2006007124A · 2006 [cited by applicant]
WO 9946398A1 · 1999 [cited by applicant]
WO 0023609A1 · 2000 [cited by applicant]
WO 0066760A1 · 2000 [cited by applicant]
WO 2005005633A2 · 2005 [cited by applicant]
WO 2006063336A2 · 2006 [cited by applicant]
WO 2006126498A1 · 2006 [cited by applicant]
WO 2007093372A1 · 2007 [cited by applicant]
WO 2008028654A1 · 2008 [cited by applicant]
WO 2008127646A2 · 2008 [cited by applicant]
WO 2011026556A1 · 2011 [cited by applicant]
Cho, B.-K., et al., “Asymmetric Synthesis of L-Homophenylalanine by Equilibrium-Shift Using Recombinant Aromatic L-Amino Acid Transaminase”, Biotechnology and Bioengineering, 83(2):226-234, 2003. [cited by applicant]
Cho, B.-K., et al., “Engineering Aromatic L-Amino Acid Transaminase for the Asymmetric Synthesis of Constrained Analogs of L-Phenylalanine”, Biotechnology And Bioengineering, 94(5):842-850, 2006. [cited by applicant]
Cho, B.-K., et al., “Enzymatic Resolution for the Preparation of Enantiomerically Enriched D-β-Heterocyclic Alanine Derivatives Using [cited by applicant]
Cho, B.-K., et al., “Redesigning the Substrate Specificity of ω-Aminotransferase for the Kinetic Resolution of Aliphatic Chiral Amines”, Biotechnology and Bioengineering, 99(2):275-284, 2008. [cited by applicant]
Cho, B.-K., et al., “Simultaneous Synthesis of Enantiomerically Pure (S)-Amino Acids and (R)-Amines Using Coupled Transaminase Reactions”, Biotechnology and Bioengineering, 81(7):783-789, 2003. [cited by applicant]
Christen, P., et al., “From Cofactor to Enzymes. The Molecular Evolution of Pyridoxal-5′-Phosphate-Dependent Enzymes”, The Chemical Record, 1:436-447, 2001. [cited by applicant]
Crump, S.P. et al., “Biocatalytic Production of Amino Acids by Transamination”, In Biocatalytic Production of Amino Acids and Derivatives; Rozzell, J. D., Wagner, F., Eds.; Wiley: New York, 1992; pp. 43-58. [cited by applicant]
C8 Eliot, A.C., et al., “The Dual-Specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation”, Biochemistry, 41:12582-12589, 2002. [cited by applicant]
Fadnavis, N.W., et al., “Asymmetric synthesis of nonproteinogenic amino acids with L-amino acid transaminase: synthesis of (2S)-2-amino-4-oxo-4-phenylbutyric and (3E,2S)-2-amino-4-phenylbutenoic acids”, Tetrahedron: Asy… [cited by applicant]
Fernandez, F.J., et al., “Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-phosphate Aminotransferase”, The Journal of Biological Chemistry, 279(20):21478-21488, 2004. [cited by applicant]
Goto, M., et al., “Crystal Structures of Branched-Chain Amino Acid Aminotransferase Complexed with Glutamate and Glutarate: True Reaction Intermediate and Double Substrate Recognition of the Enzyme”, Biochemistry, 42:37… [cited by applicant]
Haruyama, K., et al., “Structures of [cited by applicant]
Hirotsu, K., et al., “Dual Substrate Recognition of Aminotransferases”, The Chemical Record, 5:160-172, 2005. [cited by applicant]
Höhne, M., et al., “Efficient Asymmetric Synthesis of Chiral Amines by Combining Transaminase and Pyruvate Decarboxylase”, ChemBioChem, 9:363-365, 2008. [cited by applicant]
Hwang, B.-Y., et al., “High-throughput screening method for the identification of active and enantioselective ω-transaminases”, Enzyme and Microbial Technology, 34:429-436, 2004. [cited by applicant]
Hwang, B.-Y., et al., “Revisit of aminotransferase in the genomic era and its application to biocatalysis”, Journal of Molecular Catalysis B: Enzymatic, 37:47-55, 2005. [cited by applicant]
Hwang, J.-Y., et al., “Simultaneous Synthesis of 2-Phenylethanol and L-Homophenylalanine Using Aromatic Transaminase With Yeast Ehrlich Pathway”, Biotechnology and Bioengineering, 102(5):1323-1329, 2009. [cited by applicant]
Käck, H., et al., “Crystal Structure of Diaminopelargonic Acid Synthase: Evolutionary Relationships between Pyridoxal-5′-phosphate-dependent Enzymes”, J. Mol. Biol., 291:857-876, 1999. [cited by applicant]
Koszelewski, D., et al., “Asymmetric Synthesis of Optically Pure Pharmacologically Relevant Amines Employing ω-Transaminases”, Adv. Synth. Catal., 350:2761-2766, 2008. [cited by applicant]
Koszelewski, D., et al., “Deracemisation of α-Chiral Primary Amines by a One-Pot, Two-Step Cascade Reaction Catalysed by ω-Transaminases”, Eur. J. Org. Chem., pp. 2289-2292, 2009. [cited by applicant]
Koszelewski, D., et al., “Formal Asymmetric Biocatalytic Reductive Amination”, Agnew. Chem. Int. Ed., 47:9337-9340, 2008. [cited by applicant]
Koszelewski, D., et al., “Synthesis of Optically Active Amines Employing Recombinant ω-Transaminases in [cited by applicant]
Liu, W., et al., “Crystal Structures of Unbound and Aminooxyacetate-Bound [cited by applicant]
Liu, W., et al., “Kinetic and Crystallographic Analysis of Active Site Mutants of [cited by applicant]
Matsui, I., et al., “The Molecular Structure of Hyperthermostable Aromatic Aminotransferase with Novel Substrate Specificity from Pyrococcus horikoshii”, The Journal of Biological Chemistry, 275(7): 4871-4879, 2000. [cited by applicant]
Mihara, H., et al., “N-Methyl-L-amino acid dehydrogenase from Pseudomonas putida. A novel member of an unusual NAD(P)-dependent oxidoreductase superfamily”, FEBS Journal, 272:1117-1123, 2005. [cited by applicant]
Nobe, Y., et al., “The Novel Substrate Recognition Mechanism Utilized by Aspartate Aminotransferase of the Extreme Thermophile Thermus thermophilus HB8”, The Journal of Biological Chemistry, 273(45):29554-29564, 1998. [cited by applicant]
Noland, B.W., et al., “Structural Studies of Salmonella typhimurium ArnB (PmrH) Aminotransferase: A 4-Amino-4-Deoxy-L-Arabinose Lipopolysaccharide-Modifying Enzyme”, Structure, 10:1569-1580, 2002. [cited by applicant]
Okada, K., et al., “Structures of [cited by applicant]
Okada, K., et al., “Three-Dimensional Structure of [cited by applicant]
Okamoto, A., et al., “Crystal Structures of Paracoccus denitrificans Aromatic Amino Acid Aminotransferase: A Substrate Recognition Site Constructed by Rearrangement of Hydrogen Bond Network”, J. Mol. Biol., 280:443-461,… [cited by applicant]
Okamoto, A., et al., “The Active Site of Paracoccus denitrificans Aromatic Amino Acid Aminotransferase Has Contrary Properties: Flexibility and Rigidity”, Biochemistry, 38:1176-1184, 1999. [cited by applicant]
Que, S., et al., “Paracoccus denitrificans Aromatic Amino Acid Aminotransferase: A Model Enzyme for the Study of Dual Substrate Recognition Mechanism”, J. Biochem, 121:161-171, 1997. [cited by applicant]
Peisach, D., et al., “Crystallographic Study of Steps along the Reaction Pathway of D-Amino Acid Aminotransferase”, Biochemistry, 37:4958-4967, 1998. [cited by applicant]
Sandmark, J., et al., “Conserved and Nonconserved Residues in the Substrate Binding Site of 7,8-Diaminopelargonic Acid Synthase from Escherichia coli Are Essential for Catalysis”, Biochemistry, 43:1213-1222, 2004. [cited by applicant]
Sandmark, J., et al., “Structural Basis for the Inhibition of the Biosynthesis of Biotin by the Antibiotic Amiclenomycin”, The Journal of Biological Chemistry, 277(45):43352-43358, 2002. [cited by applicant]
Shin J.-S., et al., “Purification, characterization, and molecular cloning of a novel amine: pyruvate transaminase from Vibrio fluvialis JS17”, Appl. Microbiol. Biotechnol., 61:463-471, 2003. [cited by applicant]
Shin, J.-S., et al., “Asymmetric Synthesis of Chiral Amines With w-Transaminase”, Biotechnology and Bioengineering, 65(2):206-211, 1999. [cited by applicant]
Shin, J.-S., et al., “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”, … [cited by applicant]
Sivaraman, J., et al., “Crystal Structure of Histidinol Phosphate Aminotransferase (HisC) from [cited by applicant]
Sugio, S., et al., “Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 Å resolution: implication of the structural role of Leu201 in transamination”, Protein Engineering, 11(8):613-619, 1998. [cited by applicant]
Taylor, P.P., et al., “Novel biosynthetic approaches to the production of unnatural amino acids using transaminases”, Tibtech, 16:412-418, 1998. [cited by applicant]
Truppo, M.D., et al., “Efficient kinetic resolution of racemic amines using a transaminase in combination with an amino acid oxidase”, Chemical Communications, 2009, 2127-29. [cited by applicant]
Truppo, M.D., et al., “Efficient production of chiral amines at concentrations of 50g/L using transaminases”, Organic Process Research & Development 14: 234-237, 2010. [cited by applicant]
Truppo, M.D., et al., “Rapid determination of both the activity and enantioselectivity of ketoreductases”, Angew. Chem. Int. Ed. Engl., 47(14):2639-41, 2008. [cited by applicant]
Truppo, M.D., et al., “Rapid screening and scale-up of transaminase catalysed reactions,” Organic & Biomolecular Chemistry, 7:395-398, 2009. [cited by applicant]
Ura, H., et al., “Substrate Recognition Mechanism of Thermophilic Dual-Substrate Enzyme”, J. Biochem., 130:89-98, 2001. [cited by applicant]
Ura, H., et al., “Temperature Dependence of the Enzyme-Substrate Recognition Mechanism”, J. Biochem., 129:173-178, 2001. [cited by applicant]
Van Ophem, P.W., et al., “Effects of the E177K Mutation in D-Amino Acid Transaminase. Studies on an Essential Coenzyme Anchoring Group That Contributes to Stereochemical Fidelity”, Biochemistry, 38:1323-1331, 1999. [cited by applicant]
Yonaha, K., et al., “Properties of the Bound Coenzyme and Subunit Structure of ω-Amino Acid: Pyruvate Aminotransferase”, The Journal of Biological Chemistry, 258(4):2660-2665, 1983. [cited by applicant]
Yun, H., et al., “Asymmetric synthesis of (S)-α-methylbenzylamine by recombinant [cited by applicant]
Yun, H., et al., “Kinetic Resolution of (R,S)-sec-Butylamine Using Omega-Transaminase From Vibrio fluvialis JS17 Under Reduced Pressure”, Biotechnology and Bioengineering, 87(6):772-778, 2004. [cited by applicant]
Yun, H., et al., “Synthesis of Enantiomerically Pure trans-(1R,2R)- and cis-(1S,2R)-1-Amino-2-Indanol by Lipase and ω-Transaminase”, Biotechnology and Bioengineering, 93(2):391-395, 2006. [cited by applicant]
Yun, H., et al., “Use of Enrichment Culture for Directed Evolution of the Vibrio fluvialis JS17 ω-Transaminase, Which Is Resistant to Product Inhibition by Aliphatic Ketones”, Applied and Environmental Microbiology, 71(… [cited by applicant]
Yonaha, K. et al., “Monamine Transamination Catalyzed by omega-Amino Acid: Pyruvate Aminotransferase of [cited by applicant]
Matcham, G.W. et al., “Biocatalysis for Chiral Intermediates: Meeting Commercial and Technical Challenges,” CHIMICA OGGI/chemistry today, 1996. [cited by applicant]
Iwasaki, A., et al., “Microbial synthesis of chiral amines by (R)-specific transamination with [cited by applicant]
Iwasaki, A., et al., “Microbial synthesis of (R)- and (S)-3,4-dimethoxyamphetamines through stereoselective transamination”, Biotechnology Letters, 24: 1845-1846, 2003. [cited by applicant]
Genbank Accession No. ABA47738.1 GI7657826.3 dated Sep. 30, 2005. [cited by applicant]
Genbank Accession No. CAP44385.1 GI163262083 dated Dec. 18, 2007. [cited by applicant]
Genbank Accession No. YP002257813.1 GI207739420 dated Oct. 1, 2008. [cited by applicant]
Hwang, B.-Y., et al., “Identification of w-Aminotransferase from Caulobacter crescentus and Site Directed Mutagenesis to Broader Substrate Specificity,” J. Microbiol. Biotechnol. 18(1): 48-54, 2008. [cited by applicant]
Kaulmann, U. et al., “Substrate spectrum of w-transaminase from Chromobacterium violaceum DSM30191 and its potential for biocatalysis,” Enzyme Microbial Technol., 41:628-637, 2007. [cited by applicant]
Mehta, P., et al., “Aminotransferases: demonstration of homology and division into evolutionary subgroups,” Eur. J. Biochem., 214(2): 549-61, 1993. [cited by applicant]
Patel, R., et al., “Biocatalytic preparation of a chiral synthon for a vasopeptidase inhibitor: enzymatic conversion of N2-[(N-phenylmethoxy) carbonyl-L-homocysteinyl]-L-lysine(1-19)-disulfide to [4S-(4l, 7l, 10aJ)]1-oc… [cited by applicant]
Sayer, C., et al., “Crystallization and preliminary X-ray diffraction analysis of w-amino acid:pyruvate transaminase from Chromobacterium violaeceum,” Acta Cryst. F63:117-19, 2007. [cited by applicant]
Shin, J.-S., et al., “Comparison of the w-transaminases from Different Microorganisms and Application to Production of Chiral Amines,” Biosci. Biotechnol. Biochem. 65:1782-88, 2001. [cited by applicant]
Yano, T., et al., “Directed evolution of an aspartate aminotransferase with new substrate specificities,” Proc. Natl. Acad. Sci. USA, 95:5511-15, 1998. [cited by applicant]
Yi, S.-S., et al., “Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads,” Process Biochem., 42(5):895-98, 2007. [cited by applicant]
Yun, H., et al., “ω-Amino Acid: Pyruvate Transaminase from Alcaligenes denitrificans Y2k-2: a New Catalyst for Kinetic Resolution of β-Amino Acids and Amines,” Appl. Environ. Microbiol., 70(4):2529-34, 2004. [cited by applicant]
Yonaha, K., et al., “Distribution of ω-Amino Acid: Pyruvate Transaminase and Aminobutyrate: α-Ketoglutarate Transaminase in Microorganisms,” Agric. Biol. Chem., 47(10): 2257-65, 1983. [cited by applicant]
Truppo, M.D., “Rapid Screening and Process Development of Biocatalytic Reactions”, Thesis submitted Univ. of Manchester, Faculty of Engineering and Physical Sciences, 1-296, 2009. [cited by applicant]