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Substrate specificity of penicillin acylase from Streptomyces lavendulae.

Abstract：

:The kinetic parameters of several substrates of penicillin acylase from Streptomyces lavendulae have been determined. The enzyme hydrolyses phenoxymethyl penicillin (penicillin V) and other penicillins with aliphatic acyl-chains such as penicillin F, dihydroF, and K. The best substrate was penicillin K (octanoyl penicillin) with a k(cat)/K(m) of 165.3 mM(-1) s(-1). The enzyme hydrolyses also chromogenic substrates as NIPOAB (2-nitro-5-phenoxyacetamido benzoic acid), NIHAB (2-nitro-5-hexanoylamido benzoic acid) or NIOAB (2-nitro-5-octanoylamido benzoic acid), however failed to hydrolyse phenylacetil penicillin (penicillin G) or NIPAB (2-nitro-5-phenylacetamido benzoic acid) and penicillins with polar substituents in the acyl moiety. These results suggest that the structure of the acyl moiety of the substrate is more determinant than the amino moiety for enzyme specificity. The enzyme was inhibited by several organic acids and the extent of inhibition changed with the hydrophobicity of the acid. The best inhibitor was octanoic acid with a K(i) of 0.8 mM. All the results, taking together, point to an active site highly hydrophobic for this penicillin acylase from Streptomyces lavendulae.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Torres-Guzmán R,de la Mata I,Torres-Bacete J,Arroyo M,Castillón MP,Acebal C

doi

10.1006/bbrc.2002.6485

subject

Has Abstract

pub_date

2002-03-01 00:00:00

pages

593-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X02964855

journal_volume

291

pub_type

杂志文章

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