Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme

被引：27

作者：

Celis, Arianna I. ^{[1
]}

DuBois, Jennifer L. ^{[1
]}

机构：

[1] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2015年 / 574卷

基金：

美国国家卫生研究院;

关键词：

Heme; Chlorite dismutase; Heme biosynthesis; Aldoxime dehydratase; EfeB; IsdG; Heme oxygenase; DYE-DECOLORIZING PEROXIDASE; STAPHYLOCOCCUS-AUREUS ISDG; CHLORITE DISMUTASE; CRYSTAL-STRUCTURE; ALDOXIME DEHYDRATASE; CATALYTIC MECHANISM; DEGRADING ENZYMES; COUPLED OXIDATION; DEGRADATION; ENVIRONMENT;

D O I：

10.1016/j.abb.2015.03.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

PFam Clan 0032, also known as the CDE superfamily, is a diverse group of at least 20 protein families sharing a common alpha,beta-barrel domain. Of these, six different groups bind heme inside the barrel's interior, using it alternately as a cofactor, substrate, or product. Focusing on these six, an integrated picture of structure, sequence, taxonomy, and mechanism is presented here, detailing how a single structural motif might be able to mediate such an array of functions with one of nature's most important small molecules. (C) 2015 Elsevier Inc. All rights reserved.

引用

页码：3 / 17

页数：15

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