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Archives of Biochemistry and Biophysics

Volumn 402, Issue 1, 2002, Pages 1-13

The 4-oxalocrotonate tautomerase family of enzymes: How nature makes new enzymes using a β-α-β structural motif

(1) Whitman, Christian P a

a UNIVERSITY OF TEXAS AT AUSTIN (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 OXALOCROTONATE TAUTOMERASE; ACRYLIC ACID DERIVATIVE; AMINO ACID; ARGININE; AROMATIC HYDROCARBON; CARBON; CROTONIC ACID DERIVATIVE; ISOMERASE; MONOMER; PROLINE; UNCLASSIFIED DRUG; WATER;

AMINO TERMINAL SEQUENCE; BACILLUS SUBTILIS; CATALYSIS; CRYSTALLOGRAPHY; ENERGY; ENVIRONMENT; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE AMPLIFICATION; HYDROPHOBICITY; ISOMER; ISOMERISM; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PLASMID; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; SEQUENCE HOMOLOGY; SHORT SURVEY; SITE DIRECTED MUTAGENESIS;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 0036612878 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/S0003-9861(02)00052-8 Document Type: Article

Times cited : (103)

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