Characterization of the side-chain hydroxyl moieties of residues Y56, Y111, Y238, Y338, and S339 as determinants of specificity in E. coli cystathionine β-lyase

Biochemistry

Volumn 50, Issue 45, 2011, Pages 9876-9885

  Lodha, Pratik H ^a   Aitken, Susan M ^a  

^a CARLETON UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINO GROUP; AMINOETHOXYVINYLGLYCINE; CARBOXYLATE GROUPS; CATALYTIC BASE; COFACTORS; E. COLI; HYDROXYL MOIETY; ORDERS OF MAGNITUDE; PYRUVATES; SIDE-CHAINS;

AMINO ACIDS; CARBOXYLATION; HYDROLYSIS;

ESCHERICHIA COLI;

AMINOETHOXYVINYLGLYCINE; CYSTATHIONINE BETA LYASE; GLYCINE DERIVATIVE; PHENYLALANINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME SPECIFICITY; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; KINETICS; LYASES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 80755122900     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201090n     Document Type: Article

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