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5.1.1.15 |
Activity |
5.1.1.15 |
Description |
2-aminohexano-6-lactam racemase |
Notes |
Family built around the functionally-validated sequence from Achromobacter obae. The sequence from Ochrobactrum anthropi is patented. |
PDB |
3DXV; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
10 |
Sequences in seed alignment |
|
Reference sequence |
Q7M181 |
Domain interval |
20-389 |
Catalytic site |
267 K |
| |
References |
Matsui D, Fuhshuku KI, Nagamori S, Takata M, Asano Y (2017) Isolation and characterization of racemase from Ensifer sp. 23-3 that acts on α-aminolactams and α-amino acid amides J Ind Microbiol Biotechnol 44 1503-1510. Okazaki S, Suzuki A, Mizushima T, Kawano T, Komeda H, Asano Y, Yamane T. (2009) The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae Biochemistry 48 941-50. Asano Y, Yamaguchi S. (2005) Dynamic kinetic resolution of amino acid amide catalyzed by D-aminopeptidase and alpha-amino-epsilon-caprolactam racemase J Am Chem Soc 127 7696-7. Asano Y, Yamaguchi S. (2005) Discovery of amino acid amides as new substrates for α-amino--caprolactam racemase from Achromobacter obae Journal of Molecular Catalysis B: Enzymatic 36 22-29. Nakamura, N.; Oshihara, W.; Yanai,A. (1987) alpha-Amino-epsilon-caprolactam racemase for L-lysine production BIOCHEMISTRY OF VITAMIN B6 (Korpela,T. and Christen, P. Eds.) Birkhauser Verlag 449-452. Articles on 5.1.1.15 |
last changed |
2009/05/18 15:34 |
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