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- Title
A Novel α-Amino-Acid Esterase from Bacillus mycoides Capable of Forming Peptides of DD- and DL-Configurations.
- Authors
Sugihara, Akio; Shimada, Yuji; Sugihara, Shigeo; Nagao, Toshihiro; Watanabe, Yomi; Tominaga, Yoshio
- Abstract
A novel α-amino-acid esterase possessing some properties favorable for the synthesis of d-amino acid-containing peptides has been purified from the culture broth of Bacillus mycoides. The enzyme consisted of 4 subunits of 39 kDa, had an isoelectric point of 7.0, and showed its maximum activity at around 47°C and pH 7.6. The enzyme activity was strongly depressed by phenylmethanesulfonyl fluoride, but not by penicillin G or ampi-cillin, suggesting that the protein is a serine enzyme lacking penicillin-binding ability. The enzyme hydrolyzed a variety of d- and l-amino acid methyl esters with concomitant formation of homooligomers from d-Phe, d-Trp, d-Tyr, and D-Asp(OCH3) methyl esters, but it did not act on the d- or l-amino acid amides tested. Incubation of a mixture of Ac-d-Phe-OMe and d-/l-Leu-NH2 with the enzyme yielded Ac-d-Phe-d/l-Leu-NH2 together with Ac-d-Phe-OH, the hydrolysate of the carboxyl component. To its credit, the enzyme failed to hydrolyze casein as well as peptides including diastereomers of diphenylala-nine and dialanine, indicating that the enzyme would not cause secondary hydrolysis of once-formed peptides. These observations indicate the potential utility of the newly isolated enzyme for the synthesis of d-amino acid-containing peptides.
- Subjects
AMINO acids; ESTERASES; NOCARDIA corallina; ANTIBACTERIAL agents; AMIDES
- Publication
Journal of Biochemistry, 2001, Vol 130, Issue 1, p119
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a002949