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Literature DB >> 7986057

Identification of a heroin esterase in Rhodococcus sp. strain H1.

G W Cameron¹, K N Jordan, P J Holt, P B Baker, C R Lowe, N C Bruce.

Abstract

A strain of a Rhodococcus sp. (termed H1) capable of utilizing heroin as its sole carbon and energy source was isolated by selective enrichment. An inducible heroin esterase was partially purified and shown to catalyze the hydrolysis of both of the acetylester groups of heroin. The enzyme displays optimum activity at pH 8.5 and appears to be a trimer of identical subunits with an M(r) or 39,000 and a native M(r) of 120,000.

Entities: Chemical Species

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Year: 1994 PMID： 7986057 PMCID： PMC201902 DOI： 10.1128/aem.60.10.3881-3883.1994

Source DB: PubMed Journal: Appl Environ Microbiol ISSN： 0099-2240 Impact factor: 4.792

9 in total

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Authors: N C Bruce; C J Wilmot; K N Jordan; A E Trebilcock; L D Gray Stephens; C R Lowe
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Journal: Biochem J Date: 1991-03-15 Impact factor: 3.857

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Authors: D L Willey; D A Caswell; C R Lowe; N C Bruce
Journal: Biochem J Date: 1993-03-01 Impact factor: 3.857

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Journal: J Chromatogr Date: 1979-04-01

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Authors: H Sobek; H Görisch
Journal: Biochem J Date: 1988-03-01 Impact factor: 3.857

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Authors: P Andrews
Journal: Biochem J Date: 1964-05 Impact factor: 3.766

9 in total

5 in total

1. Molecular analysis of the Rhodococcus sp. strain H1 her gene and characterization of its product, a heroin esterase, expressed in Escherichia coli.

Authors: D A Rathbone; P J Holt; C R Lowe; N C Bruce
Journal: Appl Environ Microbiol Date: 1997-05 Impact factor: 4.792