Molecular Mechanisms of Enzyme Activation by Monovalent Cations

被引:73
作者
Gohara, David W. [1 ]
Di Cera, Enrico [1 ]
机构
[1] St Louis Univ, Sch Med, Edward A Doisy Dept Biochem & Mol Biol, St Louis, MO 63104 USA
基金
美国国家卫生研究院;
关键词
ALPHA-KETOACID DEHYDROGENASE; MUSCLE PYRUVATE-KINASE; CRYSTAL-STRUCTURE; NA+ BINDING; ACTIVE-SITE; 3-DIMENSIONAL STRUCTURE; ALLOSTERIC REGULATION; METAL-IONS; BETA-GALACTOSIDASE; CATALYTIC-ACTIVITY;
D O I
10.1074/jbc.R116.737833
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
Regulation of enzymes through metal ion complexation is widespread in biology and underscores a physiological need for stability and high catalytic activity that likely predated proteins in the RNA world. In addition to divalent metals such as Ca2+, Mg2+, and Zn2+, monovalent cations often function as efficient and selective promoters of catalysis. Advances in structural biology unravel a rich repertoire of molecular mechanisms for enzyme activation by Na+ and K+. Strategies range from short-range effects mediated by direct participation in substrate binding, to more distributed effects that propagate long-range to catalytic residues. This review addresses general considerations and examples.
引用
收藏
页码:20840 / 20848
页数:9
相关论文
共 100 条
[1]   Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease [J].
AEvarsson, A ;
Chuang, JL ;
Wynn, RM ;
Turley, S ;
Chuang, DT ;
Hol, WGJ .
STRUCTURE, 2000, 8 (03) :277-291
[2]   Activation of ribokinase by monovalent cations [J].
Andersson, CE ;
Mowbray, SL .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 315 (03) :409-419
[3]   The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution [J].
Ban, N ;
Nissen, P ;
Hansen, J ;
Moore, PB ;
Steitz, TA .
SCIENCE, 2000, 289 (5481) :905-920
[4]   Calcium signalling remodelling and disease [J].
Berridge, Michael J. .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2012, 40 :297-309
[5]  
Boyer Paul D., 1942, JOUR BIOL CHEM, V146, P673
[6]   Murine thrombin lacks Na+ activation but retains high catalytic activity [J].
Bush, LA ;
Nelson, RW ;
Di Cera, E .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (11) :7183-7188
[7]   STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE [J].
CHAN, MK ;
MUKUND, S ;
KLETZIN, A ;
ADAMS, MWW ;
REES, DC .
SCIENCE, 1995, 267 (5203) :1463-1469
[8]   Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase [J].
Ciszak, EM ;
Korotchkina, LG ;
Dominiak, PM ;
Sidhu, S ;
Patel, MS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (23) :21240-21246
[9]   Residue 225 determines the Na+-induced allosteric regulation of catalytic activity in serine proteases [J].
Dang, QD ;
DiCera, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (20) :10653-10656
[10]   Effect of Na+ binding on the conformation, stability and molecular recognition properties of thrombin [J].
De Filippis, V ;
De Dea, E ;
Lucatello, F ;
Frasson, R .
BIOCHEMICAL JOURNAL, 2005, 390 :485-492