Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase

Biochemistry

Volumn 44, Issue 6, 2005, Pages 1816-1823

  Wise, Eric L ^a   Yew, Wen Shan ^b   Akana, Julie ^b   Gerlt, John A ^b   Rayment, Ivan ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ESCHERICHIA COLI; MUTAGENESIS; ORGANIC COMPOUNDS; REACTION KINETICS;

ACTIVE SITES; HISTIDINE RESIDUES; LIGANDS; PROTONATIONS;

ENZYMES;

3 KETO LEVO GULONATE 6 PHOSPHATE DECARBOXYLASE; HISTIDINE; LIGAND; MAGNESIUM; OROTIDINE 5' PHOSPHATE DECARBOXYLASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CATALYST; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; METHYLOMONAS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION ANALYSIS; STRUCTURE ANALYSIS; WILD TYPE;

ALANINE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; BINDING SITES; CARBOXY-LYASES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; GLUTAMIC ACID; MUTAGENESIS, SITE-DIRECTED; OROTIDINE-5'-PHOSPHATE DECARBOXYLASE; RIBULOSEPHOSPHATES; SUBSTRATE SPECIFICITY; THREONINE;

ESCHERICHIA COLI; METHYLOMONAS AMINOFACIENS;

EID: 13544274134     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0478143     Document Type: Article

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