来自“嗜糖栖热放线菌”的β-甘露聚糖酶是一种多结构域酶的一部分。
The beta-mannanase from "Caldocellum saccharolyticum" is part of a multidomain enzyme.
作者信息
Gibbs M D, Saul D J, Lüthi E, Bergquist P L
机构信息
Department of Cellular & Molecular Biology, University of Auckland, New Zealand.
出版信息
Appl Environ Microbiol. 1992 Dec;58(12):3864-7. doi: 10.1128/aem.58.12.3864-3867.1992.
Abstract
The complete sequence of a beta-mannanase gene from an anaerobic extreme thermophile was determined, and it shows that the expressed protein consists of two catalytic domains and two binding domains separated by spacer regions rich in proline and threonine residues. The amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase. Neither domain shows homology with any other cellulase or hemicellulase sequence at the nucleic acid or protein level.
摘要
测定了来自一种厌氧极端嗜热菌的β-甘露聚糖酶基因的完整序列，结果表明表达的蛋白质由两个催化结构域和两个结合结构域组成，它们被富含脯氨酸和苏氨酸残基的间隔区隔开。氨基末端催化结构域具有β-甘露聚糖酶活性，羧基末端结构域起内切葡聚糖酶的作用。在核酸或蛋白质水平上，这两个结构域均与任何其他纤维素酶或半纤维素酶序列无同源性。
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