Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: Movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria

Journal of Molecular Biology

Volumn 397, Issue 5, 2010, Pages 1261-1275

  Ramón Maiques, Santiago ^a   Marina, Alberto ^a   Guinot, Anna ^a   Gil Ortiz, Fernando ^a   Uriarte, Matxalen ^a   Fita, Ignacio ^b   Rubio, Vicente ^a  

^a CENTRO DE INVESTIGACIÓN BIOMÉDICA EN RED DE ENFERMEDADES RARAS CIBERER   (Spain)

^b INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

Author keywords

Amino acid kinase family; Induced fit; Kinase mechanisms; Phosphoryl group transfer; X ray crystal structure

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CARBAMATE KINASE; CARBAMOYL PHOSPHATE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENTEROCOCCUS FAECALIS; ENZYME ACTIVE SITE; ENZYME BINDING; FERMENTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

ENTEROCOCCUS FAECALIS;

EID: 77950517828     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.038     Document Type: Article

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