Structural and functional features of dimeric dihydrodiol dehydrogenase

被引：24

作者：

Carbone, V. ^{[1
]}

Hara, A. ^{[2
]}

El-Kabbani, O. ^{[1
]}

机构：

[1] Monash Univ, Dept Med Chem, Victorian Coll Pharm, Parkville, Vic 3052, Australia

[2] Gifu Pharmaceut Univ, Biochem Lab, Gifu 5028585, Japan

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2008年 / 65卷 / 10期

关键词：

dihydrodiol dehydrogenase; oxido-reductases; site-directed mutagenesis; crystal structure; molecular modeling;

D O I：

10.1007/s00018-008-7508-5

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：

Dimeric dihydrodiol dehydrogenase ( DD) catalyzes the NADP(+)- dependent oxidation of trans-dihydrodiols of aromatic hydrocarbons to their corresponding catechols. The tertiary structure of dimeric DD concists of a classical dinucleotide binding domain comprising two beta alpha beta alpha beta motifs at the N-terminus, and an eight-stranded, predominantly antiparallel sheet, forming the C-terminal domain The aim of this reviewis to summarize the biochemical and structural properties of dimeric DD, compare it to enzymes that are structurally similar, and provide an insight into its catalytic mechanism and membership amongst a unique family of monomeric/oligomeric proteins that most likely share a common ancestry.

引用

页码：1464 / 1474

页数：11

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