The product of the natural reaction catalyzed by 4-oxalocrotonate tautomerase becomes an affinity label of its mutant

Bioorganic and Medicinal Chemistry

Volumn 10, Issue 12, 2002, Pages 3891-3897

  Brik, Ashraf ^a,b   Dawson, Philip E ^a   Keinan, Ehud ^a,b  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXO 3 HEXENEDIOATE; 2 OXOACID; 4 OXALOCROTONATE; 4 OXALOCROTONATE TAUTOMERASE; ENZYME; MUTANT PROTEIN; NATURAL PRODUCT; PROLINE; UNCLASSIFIED DRUG;

ACID BASE BALANCE; AFFINITY LABELING; ALKYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CHEMICAL BOND; CHEMICAL MODIFICATION; CHEMICAL REACTION; COVALENT BOND; ISOMERISM; MASS SPECTROMETRY; MICHAEL ADDITION; REDUCTION;

AFFINITY LABELS; ALKYLATION; AMINO ACID SEQUENCE; CATALYSIS; DECARBOXYLATION; HYDROLYSIS; IMINES; ISOMERASES; KINETICS; MUTAGENESIS, SITE-DIRECTED; MUTATION; PSEUDOMONAS PUTIDA; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0036973289     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(02)00385-1     Document Type: Article

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