Substrate specificity of the highly alkalophilic bacterial proteinase esperase: relation to the x-ray structure.
Curr Microbiol
; 42(5): 368-71, 2001 May.
Article
in En
| MEDLINE
| ID: mdl-11400059
ABSTRACT
Esperase is a highly alkalophilic bacterial proteinase produced by Bacillus lentus. The enzyme hydrolyzes peptide bonds comprising the carboxylic groups of hydrophobic as well as hydrophilic residues in the oxidized insulin B chain. Some of these bonds are not attacked by other alkaline microbial proteinases. P1-P4 specificity was determined by a series of peptide nitroanilides. The S1 recognition loop exhibits a preference for Phe. The "cleft" of the smallest subsite S2 prefers Ala and exhibits low affinity for the larger chain of Leu. S3 is more open than the other subsites and can accept a variety of residues. Hydrophobic interactions predominate in the S4-P4 interactions because S4 can accommodate Phe very well. The results characterize Esperase as an endopeptidase with a broader specificity in comparison with other microbial serine proteinases. This is probably owing to a more flexible substrate binding site.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacillus
/
Serine Endopeptidases
/
Insulin
/
Anilides
Language:
En
Journal:
Curr Microbiol
Year:
2001
Document type:
Article
Affiliation country: