Mapping active site residues in glutamate-5-kinase. The substrate glutamate and the feed-back inhibitor proline bind at overlapping sites

FEBS Letters

Volumn 580, Issue 26, 2006, Pages 6247-6253

  Pérez Arellano, Isabel ^a   Rubio, Vicente ^b   Cervera, Javier ^a  

^a CENTRO DE INVESTIGACIÓN PRÍNCIPE FELIPE   (Spain)

^b INSTITUTO DE BIOMEDICINA DE VALENCIA   (Spain)

Author keywords

glutamyl 5 kinase; Allosteric regulation; Amino acid kinase; Glutamate 5 kinase; Phosphoryl group transfer; proB; Proline synthesis; Site directed mutagenesis

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; GLUTAMATE 5 KINASE; GLUTAMIC ACID; N ACETYLGLUTAMIC ACID; PHOSPHOTRANSFERASE; PROLINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; FEEDBACK SYSTEM; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN FUNCTION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATE; AMINO ACIDS; BINDING SITES; CATALYSIS; ESCHERICHIA COLI PROTEINS; FEEDBACK, BIOCHEMICAL; GLUTAMIC ACID; MUTAGENESIS, SITE-DIRECTED; PHOSPHOTRANSFERASES (CARBOXYL GROUP ACCEPTOR); PROLINE; PROTEIN BINDING; SEQUENCE ALIGNMENT;

ESCHERICHIA COLI;

EID: 33750502699     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.10.031     Document Type: Article

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