Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: Studies on substrate specificity and inhibitor binding

Proteins: Structure, Function and Genetics

Volumn 70, Issue 2, 2008, Pages 429-441

  Rajaram, V ^a   Prasuna, P Ratna ^a   Savithri, H S ^a   Murthy, M R N ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

ArgD; Arginine metabolism; Gabaculine; Lysine biosynthesis; Pyridoxal 5 phosphate

Indexed keywords

AMINOTRANSFERASE; ARGININE; BACTERIAL ENZYME; GENOMIC DNA; GLUTAMIC ACID; LYSINE; N ACETYLORNITHINE AMINOTRANSFERASE; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG;

AMINO ACID SYNTHESIS; ARTICLE; BACTERIAL CELL WALL; BINDING AFFINITY; BINDING SITE; BIOSYNTHESIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVATION; ENZYME ASSAY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; ESCHERICHIA COLI; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; SPECTROMETER; STRUCTURE ANALYSIS;

CATALYSIS; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; HUMANS; KINETICS; PROTEIN CONFORMATION; SALMONELLA TYPHIMURIUM; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY; TRANSAMINASES;

BACTERIA (MICROORGANISMS); SALMONELLA TYPHIMURIUM;

EID: 37849030118     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21567     Document Type: Article

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