Do bacterial l-asparaginases utilize a catalytic triad Thr-Tyr-Glu?

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1550, Issue 2, 2001, Pages 117-128

  Aghaiypour, Khosrow ^a   Wlodawer, Alexander ^a   Lubkowski, Jacek ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Bacterial l asparaginase; Enzymatic mechanism; Suicide inhibitor; X ray crystallography

Indexed keywords

6 DIAZO 5 OXONORLEUCINE; ASPARAGINASE; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINASE; SERINE; THREONINE; TYROSINE;

ARTICLE; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME MECHANISM; ERWINIA; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STEREOISOMERISM; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ASPARAGINASE; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIAZOOXONORLEUCINE; ERWINIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; STEREOISOMERISM; WATER;

BACTERIA (MICROORGANISMS); ERWINIA; ERWINIA CHRYSANTHEMI; ESCHERICHIA COLI; PSEUDOMONAS; PSEUDOMONAS SP. 7A;

EID: 0035905523     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00270-9     Document Type: Article

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