An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus: high activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural l-amino acids

Enzyme and Microbial Technology

Volumn 40, Issue 5, 2007, Pages 1407-1411

  Chen, Sihong ^a   Engel, Paul C ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Biocatalysts; Co enzyme recycling; Enzyme stability; Kinetic parameters; Non natural amino acids; Organic solvents; Phenylalanine dehydrogenase (PheDH) mutants; Substrate specificity

Indexed keywords

COENZYME RECYCLING; ENZYME STABILITY; PHENYLALANINE DEHYDROGENASE (PHEDH) MUTANTS; SUBSTRATE SPECIFICITY;

ACETONITRILE; AMINO ACIDS; BIOCATALYSTS; COENZYMES; KINETIC PARAMETERS; ORGANIC SOLVENTS;

ENZYME KINETICS;

ACETONITRILE; ALCOHOL; ALCOHOL DEHYDROGENASE; BACTERIAL ENZYME; METHANOL; ORGANIC SOLVENT; PHENYLALANINE DEHYDROGENASE L307V; UNCLASSIFIED DRUG;

AMINO ACID SYNTHESIS; ARTICLE; BACILLUS SPHAERICUS; BIOCATALYST; CATALYSIS; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME KINETICS; ENZYME STABILITY; MOLECULAR STABILITY; NONHUMAN; OXIDATION KINETICS; PH MEASUREMENT; SOLVENT EFFECT; SYNTHESIS;

BACILLUS SPHAERICUS;

EID: 33847653796     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.10.021     Document Type: Article

References (11)

1. Kazlauskas R. Enzymes in focus. Nature 436 (2005) 1096-1097
2. Khmelnitsky Y.L., and Rich J.O. Biocatalysis in nonaqueous solvents. Curr. Opin. Chem. Biol. 3 (1999) 47-53
3. Castro G.R., and Knubovets T. Homogeneous biocatalysis in organic solvents and water-organic mixtures. Crit. Rev. Biotechnol. 23 (2003) 195-231
4. Nakamura K., Fujii T., Kato Y., Asano Y., and Cooper A.J.L. Quantitation of l-amino acids by substrate recycling between an aminotransferase and a dehydrogenase: application to the determination of l-phenylalanine in human blood. Anal. Biochem. 234 (1996) 19-22
5. Randell E.W., and Lehotay D.C. An automated enzymatic method on the Roche COBAS MIRA™ S for monitoring phenylalanine in dried blood spots of patients with phenylketonuria. Clin. Biochem. 29 (1996) 133-138
6. Hummel W., Weiss N., and Kula M.R. Isolation and characterisation of a bacterium possessing l-phenylalanine dehydrogenase activity. Arch. Microbiol. 137 (1984) 47-52
7. Asano Y., Yamada A., Kato K., Yamaguchi K., Hibino Y., Hirai K., et al. Enantioselective synthesis of (S)-amino acids by phenylalanine dehydrogenase from Bacillus sphaericus: use of natural and recombinant enzymes. J. Org. Chem. 55 (1990) 5567-5571
8. Seah S.Y.K., Britton K.L., Baker P.J., Rice D.W., Asano Y., and Engel P.C. Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis. FEBS Lett. 370 (1995) 93-96
9. Seah S.Y.K., Britton K.L., Rice D.W., Asano Y., and Engel P.C. Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates. Biochemistry 41 (2002) 11390-11397
10. Busca P., Paradisi F., Moynihan E., Maguire A.R., and Engel P.C. Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis. Org. Biomol. Chem. 2 (2004) 2684-2691
11. Cainelli G., Engel P.C., Galletti P., Giacomini D., Gualandi A., and Paradisi F. Engineered phenylalanine dehydrogenase in organic solvents: homogeneous and biphasic enzymatic reactions. Org. Biomol. Chem. 3 (2005) 4316-4320