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B6db families:
Description 2-aminohexano-6-lactam racemase
Notes Family built around the functionally-validated sequence from Achromobacter obae. The sequence from Ochrobactrum anthropi is patented.
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 10
Sequences in seed alignment
BacteriaWP_025424688 (Ensifer sp. 23-3); NP_386695 (Sinorhizobium meliloti); WP_044430366 (Skermanella aerolata); WP_048647021 (Ancylobacter sp. FA202); Q7M181 (Achromobacter obae); WP_004120361 (Rhizobium freirei); WP_089960733 (Citreicella thiooxidans); CAF32615 (Arthrobacter nicotianae); YP_001314044 (Sinorhizobium medicae WSM419); CAF32614 (Ochrobactrum anthropi);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence Q7M181
Domain interval 20-389
Catalytic site 267 K
 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
last changed 2009/05/18 15:34

B6db families