The structure of putative N-acetyl glutamate kinase from Thermus thermophilus reveals an intermediate active site conformation of the enzyme

Biochemical and Biophysical Research Communications

Volumn 420, Issue 3, 2012, Pages 692-697

  Sundaresan, Ramya ^a   Ragunathan, Preethi ^a   Kuramitsu, Seiki ^b,c   Yokoyama, Shigeyuki ^d,e   Kumarevel, Thirumananseri ^b   Ponnuraj, Karthe ^a  

^a UNIVERSITY OF MADRAS   (India)

^b Harima Institute ^*  (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d RIKEN YOKOHAMA INSTITUTE   (Japan)

^e UNIVERSITY OF TOKYO   (Japan)

Author keywords

Arginine biosynthesis; Catalytic cycle; Crystal structure; Intermediate conformation; N acetyl l glutamate kinase

Indexed keywords

ACETYLGLUTAMATE KINASE; ARGININE; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; MESOPHILIC BACTERIUM; PRIORITY JOURNAL; THERMOPHILIC BACTERIUM; THERMUS THERMOPHILUS;

ARGININE; CATALYTIC DOMAIN; ENZYME STABILITY; FEEDBACK, PHYSIOLOGICAL; HOT TEMPERATURE; PHOSPHOTRANSFERASES (CARBOXYL GROUP ACCEPTOR); PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMOTOGA MARITIMA; THERMUS THERMOPHILUS;

EID: 84859622203     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.072     Document Type: Article

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