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嗜冷α-淀粉酶缺失突变体在嗜盐栖冷假交替单胞菌TAC125中的分泌

Secretion of psychrophilic alpha-amylase deletion mutants in Pseudoalteromonas haloplanktis TAC125.

作者信息

Cusano Angela Maria, Parrilli Ermenegilda, Duilio Angela, Sannia Giovanni, Marino Gennaro, Tutino Maria Luisa

机构信息

Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario M.S. Angelo via Cynthia, Napoli Italia.

出版信息

FEMS Microbiol Lett. 2006 May;258(1):67-71. doi: 10.1111/j.1574-6968.2006.00193.x.

DOI:10.1111/j.1574-6968.2006.00193.x
PMID:16630257
Abstract

The nature and location of structural features responsible for the secretion of a cold-adapted alpha-amylase in the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 was studied by deletion mutagenesis of the wild-type enzyme and of chimerical proteins derived from the fusion of the alpha-amylase with a reporter enzyme. Domain C of the psychrophilic alpha-amylase contains secretion features involved in extracellular targeting.

摘要

通过对野生型酶以及由α-淀粉酶与报告酶融合产生的嵌合蛋白进行缺失诱变，研究了南极海洋细菌嗜冷栖假交替单胞菌TAC125中负责分泌冷适应α-淀粉酶的结构特征的性质和位置。嗜冷α-淀粉酶的结构域C包含参与细胞外靶向的分泌特征。

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