Mechanism of the orotidine 5′-monophosphate decarboxylase-catalyzed reaction: Evidence for substrate destabilization

Biochemistry

Volumn 48, Issue 24, 2009, Pages 5518-5531

  Chan, Kui K ^a   Wood, B McKay ^a   Fedorov, Alexander A ^b   Fedorov, Elena V ^b   Imker, Heidi J ^a   Amyes, Tina L ^c   Richard, John P ^c   Almo, Steven C ^b   Gerlt, John A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; ANIONIC INTERMEDIATES; CARBOXYLATE GROUPS; CATALYTIC EFFICIENCIES; CATALYZED REACTIONS; DECARBOXYLASE; DIFFERENTIAL EFFECT; ELECTROSTATIC INTERACTIONS; FUNCTIONAL CHARACTERIZATION; LOWER LIMITS; METHANOTHERMOBACTER THERMAUTOTROPHICUS; MONOPHOSPHATE; RATE ACCELERATION; REACTION CATALYZED; REACTIVE SUBSTRATES; SACCHAROMYCES CEREVISIAE; STRUCTURAL BASIS; TRANSITION STATE; WILD TYPES;

CARBOXYLATION; DEUTERIUM; DYES; MOLYBDENUM; MOLYBDENUM COMPOUNDS;

SUBSTRATES;

ASPARTIC ACID; CARBOXYLIC ACID; DEUTERIUM; OROTIDINE 5' PHOSPHATE DECARBOXYLASE;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; DECARBOXYLATION; ELECTRICITY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; METHANOBACTERIUM THERMOAUTOTROPHICUM; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; STRUCTURE ANALYSIS; WILD TYPE;

BACTERIAL PROTEINS; CATALYSIS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; METHANOBACTERIACEAE; MODELS, MOLECULAR; OROTIDINE-5'-PHOSPHATE DECARBOXYLASE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

METHANOTHERMOBACTER THERMAUTOTROPHICUS; SACCHAROMYCES CEREVISIAE;

EID: 67649210974     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900623r     Document Type: Article

References (39)

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