The 1.5 Å resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and a provides insight into substrate binding and stability in carbamate kinases

Journal of Molecular Biology

Volumn 299, Issue 2, 2000, Pages 463-476

  Ramón Maiques, Santiago ^a   Marina, Alberto ^a   Uriarte, Matxalen ^a   Fita, Ignacio ^b   Rubio, Vicente ^a  

^a INSTITUTO DE BIOMEDICINA DE VALENCIA   (Spain)

^b INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

Author keywords

ADP site; Arginine metabolism; Hyperthermophiles; Phosphoryl group transfer; Pyrococcus furiosus

Indexed keywords

ADENOSINE DIPHOSPHATE; CARBAMATE KINASE; CARBAMOYL PHOSPHATE SYNTHASE; CARBAMOYL PHOSPHATE; PHOSPHOTRANSFERASE; SOLVENT;

ARCHAEBACTERIUM; ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PYROCOCCUS FURIOSUS; THERMOSTABILITY; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ELECTRICITY; ENTEROCOCCUS FAECALIS; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

ARCHAEA; BACTERIA (MICROORGANISMS); PYROCOCCUS FURIOSUS;

ADENOSINE DIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; CARBAMYL PHOSPHATE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ELECTROSTATICS; ENTEROCOCCUS FAECALIS; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOTRANSFERASES (CARBOXYL GROUP ACCEPTOR); PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYROCOCCUS FURIOSUS; SOLVENTS; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

EID: 0034595434     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3779     Document Type: Article

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