The chemical versatility of the β-α-β fold: Catalytic promiscuity and divergent evolution in the tautomerase superfamily

被引：75
作者：
Poelarends, G. J. [2 ]
Veetil, V. Puthan [2 ]
Whitman, C. P. [1 ]
机构：
[1] Univ Texas Austin, Coll Pharm, Div Med Chem, Austin, TX 78712 USA
[2] Univ Groningen, Groningen Res Inst Pharm, Dept Pharmaceut Biol, NL-9713 AV Groningen, Netherlands
来源：
CELLULAR AND MOLECULAR LIFE SCIENCES | 2008年 / 65卷 / 22期
关键词：
Tautomerase superfamily; divergent evolution; catalytic promiscuity;
D O I：
10.1007/s00018-008-8285-x
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：
Tautomerase superfamily members have an amino-terminal proline and a beta-alpha-beta fold, and include 4-oxalocrotonate tautomerase (4-OT), 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI), trans- and cis-3-chloroacrylic acid dehalogenase (CaaD and cis-CaaD, respectively), malonate semialdehyde decarboxylase (MSAD), and macrophage migration inhibitory factor (MIF), which exhibits a phenylpyruvate tautomerase (PPT) activity. Pro-1 is a base (4-OT, CHMI, the PPT activity of MIF) or an acid (CaaD, cis-CaaD, MSAD). Components of the catalytic machinery have been identified and mechanistic hypotheses formulated. Characterization of new homologues shows that these mechanisms are incomplete. 4-OT, CaaD, cis-CaaD, and MSAD also have promiscuous activities with a hydratase activity in CaaD, cis-CaaD, and MSAD, PPT activity in CaaD and cis-CaaD, and CaaD and cis-CaaD activities in 4-OT. The shared promiscuous activities provide evidence for divergent evolution from a common ancestor, give hints about mechanistic relationships, and implicate catalytic promiscuity in the emergence of new enzymes.
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收藏
页码：3606 / 3618
页数：13
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