Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli

Acta Crystallographica Section D: Biological Crystallography

Volumn 60, Issue 6, 2004, Pages 1173-1176

  Prahl, Adam ^a   Pazgier, Marzena ^a   Hejazi, Mahdi ^b   Lockau, Wolfgang ^b   Lubkowski, Jacek ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b HUMBOLDT UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

ASPARAGINASE; BETA ASPARTYL PEPTIDASE; BETA-ASPARTYL PEPTIDASE; CATION; DIPEPTIDASE; ION; METAL; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE; SODIUM;

ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; HYDROLYSIS; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ASPARAGINASE; ASPARTYLGLUCOSYLAMINASE; BINDING SITES; CATALYSIS; CATIONS; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDASES; ESCHERICHIA COLI; HYDROLYSIS; IONS; METALS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SODIUM;

EID: 16644374971     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444904003403     Document Type: Article

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