The mechanism of the reaction catalyzed by uronate isomerase illustrates how an isomerase may have evolved from a hydrolase within the amidohydrolase superfamily

Biochemistry

Volumn 48, Issue 37, 2009, Pages 8879-8890

  Nguyen, Tinh T ^a   Fedorov, Alexander A ^b   Williams, LaKenya ^a   Fedorov, Elena V ^b   Li, Yingchun ^a   Xu, Chengfu ^a   Almo, Steven C ^b   Raushel, Frank M ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE STRUCTURE; AMIDOHYDROLASE SUPERFAMILY; BACILLUS HALODURANS; CARBONYL GROUPS; CATALYTIC ACTIVITY; CHEMICAL MECHANISM; COMBINED ACTIONS; HYDROLASES; HYDROLYTIC REACTIONS; HYDROXYL GROUPS; ISOMERASES; ISOMERIZATION REACTION; KINETIC CONSTANT; METAL CENTERS; PRIMARY ISOTOPE EFFECT; PRODUCT RELEASE; PROTONATED; RATE PROFILES; RATE-LIMITING STEPS; REACTION CATALYZED; SOLVENT VISCOSITY; X-RAY STRUCTURE;

BACTERIOLOGY; CARBOXYLATION; ELECTRON TRANSITIONS; ESCHERICHIA COLI; HYDROGEN; ISOMERS; ISOTOPES; METAL IONS; OXYGEN; PROTON TRANSFER; PROTONS; RATE CONSTANTS; REACTION KINETICS; SUBSTRATES;

ISOMERIZATION;

AMIDASE; CARBOXYLIC ACID; DIVALENT CATION; GLUCURONATE ISOMERASE; GLUCURONIC ACID; HYDROLASE; HYDROXYL GROUP; ISOMERASE; ISOTOPE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROGEN BOND; HYDROLYSIS; ISOMERIZATION; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; VISCOSITY;

ALDOSE-KETOSE ISOMERASES; AMIDOHYDROLASES; BACILLUS; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM EXCHANGE MEASUREMENT; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; MULTIGENE FAMILY; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY;

BACILLUS HALODURANS; ESCHERICHIA COLI;

EID: 70349110534     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901046x     Document Type: Article

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