Mechanisms and structures of crotonase superfamily enzymes - How nature controls enolate and oxyanion reactivity

被引:98
作者
Hamed, R. B. [1 ]
Batchelar, E. T. [1 ]
Clifton, I. J. [1 ]
Schofield, C. J. [1 ]
机构
[1] Univ Oxford, Dept Chem, Chem Res Lab, Oxford OX1 3TA, England
基金
英国生物技术与生命科学研究理事会;
关键词
crotonase superfamily; oxyanion hole; enolate intermediates; coenzyme A; beta-oxidation; proteases;
D O I
10.1007/s00018-008-8082-6
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
Structural and mechanistic studies on the crotonase superfamily (CS) are reviewed with the aim of illustrating how a conserved structural platform can enable catalysis of a very wide range of reactions. Many CS reactions have precedent in the 'carbonyl' chemistry of organic synthesis; they include alkene hydration/isomerization, aryl-halide dehalogenation, (de)carboxylation, CoA ester and peptide hydrolysis, fragmentation of beta-diketones and C-C bond formation, cleavage and oxidation. CS enzymes possess a canonical fold formed from repeated beta beta alpha units that assemble into two approximately perpendicular beta-sheets surrounded by alpha-helices. CS enzymes often, although not exclusively, oligomerize as trimers or dimers of trimers. Two conserved backbone NH groups in CS active sites form an oxyanion 'hole' that can stabilize enolate/oxyanion intermediates. The range and efficiency of known CS-catalyzed reactions coupled to their common structural platforms suggest that CS variants may have widespread utility in biocatalysis.
引用
收藏
页码:2507 / 2527
页数:21
相关论文
共 135 条
[1]   Enoyl-CoA hydratase: Reaction, mechanism, and inhibition [J].
Agnihotri, G ;
Liu, HW .
BIOORGANIC & MEDICINAL CHEMISTRY, 2003, 11 (01) :9-20
[2]   An Escherichia coli chromosomal ''addiction module'' regulated by 3',5'-bispyrophosphate: A model for programmed bacterial cell death [J].
Aizenman, E ;
EngelbergKulka, H ;
Glaser, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (12) :6059-6063
[3]   CROTONASE-CATALYZED BETA-ELIMINATION IS CONCERTED - A DOUBLE ISOTOPE EFFECT STUDY [J].
BAHNSON, BJ ;
ANDERSON, VE .
BIOCHEMISTRY, 1991, 30 (24) :5894-5906
[4]   Structural mechanism of enoyl-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted fashion [J].
Bahnson, BJ ;
Anderson, VE ;
Petsko, GA .
BIOCHEMISTRY, 2002, 41 (08) :2621-2629
[5]   GLUTAMATE GAMMA-SEMIALDEHYDE AS A NATURAL TRANSITION-STATE ANALOG INHIBITOR OF ESCHERICHIA-COLI GLUCOSAMINE-6-PHOSPHATE SYNTHASE [J].
BEARNE, SL ;
WOLFENDEN, R .
BIOCHEMISTRY, 1995, 34 (36) :11515-11520
[6]   Structural characterization of a β-diketone hydrolase from the cyanobacterium Anabaena sp PCC 7120 in native and product-bound forms, a coenzyme A-independent member of the crotonase suprafamily [J].
Bennett, Joseph P. ;
Whittingham, Jean L. ;
Brzozowski, A. Marek ;
Leonard, Philip M. ;
Grogan, Gideon .
BIOCHEMISTRY, 2007, 46 (01) :137-144
[7]   3D DOMAIN SWAPPING - A MECHANISM FOR OLIGOMER ASSEMBLY [J].
BENNETT, MJ ;
SCHLUNEGGER, MP ;
EISENBERG, D .
PROTEIN SCIENCE, 1995, 4 (12) :2455-2468
[8]   Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 angstrom resolution: An enzyme catalyst generated via adaptive mutation [J].
Benning, MM ;
Taylor, KL ;
Liu, RQ ;
Yang, G ;
Xiang, H ;
Wesenberg, G ;
DunawayMariano, D ;
Holden, HM .
BIOCHEMISTRY, 1996, 35 (25) :8103-8109
[9]   New reactions in the crotonase superfamily:: Structure of methylmalonyl CoA decarboxylase from Escherichia coli [J].
Benning, MM ;
Haller, T ;
Gerlt, JA ;
Holden, HM .
BIOCHEMISTRY, 2000, 39 (16) :4630-4639
[10]   The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme [J].
Bilder, P ;
Lightle, S ;
Bainbridge, G ;
Ohren, J ;
Finzel, B ;
Sun, F ;
Holley, S ;
Al-Kassim, L ;
Spessard, C ;
Melnick, M ;
Newcomer, M ;
Waldrop, GL .
BIOCHEMISTRY, 2006, 45 (06) :1712-1722