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淀粉水解酶及相关酶的结构域水平组织比较。

Comparison of the domain-level organization of starch hydrolases and related enzymes.

作者信息

Jespersen H M, MacGregor E A, Sierks M R, Svensson B

机构信息

Department of Chemistry, Carlsberg Laboratory, Copenhagen Valby, Denmark.

出版信息

Biochem J. 1991 Nov 15;280 ( Pt 1)(Pt 1):51-5. doi: 10.1042/bj2800051.

DOI:10.1042/bj2800051
PMID:1741756
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1130598/
Abstract

Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (beta/alpha)8-barrel and a smaller C-terminal domain as seen in crystal structures of alpha-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-alpha-1,6 linkages contain domains N-terminal to the (beta/alpha)8-barrel.

摘要

几种淀粉水解酶及相关酶的结构预测和疏水簇分析表明存在11种结构域类型。如在α-淀粉酶和环糊精葡糖基转移酶的晶体结构中所见,大多数酶具有一个催化性(β/α)8桶和一个较小的C端结构域。一些酶还具有一个淀粉颗粒结合结构域。断裂或形成α-1,6-内连接的酶在(β/α)8桶的N端含有结构域。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a4/1130598/ffdcbb31fd8b/biochemj00147-0058-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a4/1130598/ffdcbb31fd8b/biochemj00147-0058-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/68a4/1130598/ffdcbb31fd8b/biochemj00147-0058-a.jpg

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本文引用的文献

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Structure and possible catalytic residues of Taka-amylase A.高峰淀粉酶A的结构及可能的催化残基
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Identification of base mismatches recognized by the heteroduplex-DNA-repair system of Streptococcus pneumoniae.肺炎链球菌异源双链DNA修复系统识别的碱基错配鉴定。
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