红球菌属菌株H1中一种海洛因酯酶的鉴定
Identification of a heroin esterase in Rhodococcus sp. strain H1.
作者信息
Cameron G W, Jordan K N, Holt P J, Baker P B, Lowe C R, Bruce N C
机构信息
Institute of Biotechnology, University of Cambridge, United Kingdom.
出版信息
Appl Environ Microbiol. 1994 Oct;60(10):3881-3. doi: 10.1128/aem.60.10.3881-3883.1994.
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.
摘要
通过选择性富集分离出了一株能够将海洛因作为唯一碳源和能源的红球菌属菌株（称为H1）。一种可诱导的海洛因酯酶被部分纯化，并显示出能催化海洛因两个乙酰酯基团的水解。该酶在pH 8.5时表现出最佳活性，似乎是由相同亚基组成的三聚体，亚基的相对分子质量（M(r)）为39,000，天然酶的相对分子质量为120,000。
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