FUNCTIONALLY DIVERSE ENZYME SUPERFAMILY THAT ABSTRACTS THE ALPHA-PROTONS OF CARBOXYLIC-ACIDS

被引:140
作者
BABBITT, PC
MRACHKO, GT
HASSON, MS
HUISMAN, GW
KOLTER, R
RINGE, D
PETSKO, GA
KENYON, GL
GERLT, JA
机构
[1] UNIV ILLINOIS, DEPT BIOCHEM, URBANA, IL 61801 USA
[2] BRANDEIS UNIV, ROSENSTIEL BASIC MED SCI RES CTR, WALTHAM, MA 02254 USA
[3] HARVARD UNIV, SCH MED, DEPT MICROBIOL & MOLEC GENET, BOSTON, MA 02115 USA
关键词
D O I
10.1126/science.7855594
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. in this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.
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页码:1159 / 1161
页数:3
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