Structure and chemistry of 4-methylideneimidazole-5-one containing enzymes

被引：47

作者：

Cooke, Heather A. ^{[1
]}

Christianson, Carl V. ^{[1
]}

Bruner, Steven D. ^{[1
]}

机构：

[1] Boston Coll, Dept Chem, Merkert Chem Ctr, Chestnut Hill, MA 02467 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2009年 / 13卷 / 04期

关键词：

PHENYLALANINE AMMONIA-LYASE; ANTITUMOR ANTIBIOTIC C-1027; BIOSYNTHETIC GENE-CLUSTER; TYROSINE AMINOMUTASE; CRYSTAL-STRUCTURE; BIOCHEMICAL-CHARACTERIZATION; ELECTROPHILIC CENTER; MECHANISM; CATALYSIS; DEHYDROALANINE;

D O I：

10.1016/j.cbpa.2009.06.013

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：

The prosthetic group 4-methylideneimidazole-5-one (MIO) is the catalytic component of the ammonia lyase class of enzymes. This family is responsible for the processing of amino acids in a variety of metabolic pathways through the elimination of ammonia to form unsaturated products. Recently, new chemistry has been attributed to this family with the discovery of MIO-based aminomutases. The mechanism of electrophilic chemistry catalyzed by MIO-based enzymes has been investigated for several decades. Recent X-ray crystal structures of members of the family have provided novel insight into the molecular basis for catalysis and substrate recognition. In addition, the inclusion of aminomutases in natural product biosynthetic pathways has spurned recent advances toward rational engineering and chemoenzymatic applications.

引用

页码：460 / 468

页数：9

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