Structure of a novel N-acetyl-l-citrulline deacetylase from Xanthomonas campestris

Biophysical Chemistry

Volumn 126, Issue 1-3, 2007, Pages 86-93

  Shi, Dashuang ^a   Yu, Xiaolin ^a   Roth, Lauren ^b   Tuchman, Mendel ^a   Allewell, Norma M ^b  

^a CHILDREN S RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF MARYLAND   (United States)

Author keywords

ArgE gene; Arginine biosynthesis; Crystal structure; Deacetylase; N acetyl l citrulline; N acetyl l ornithine

Indexed keywords

ACETIC ACID DERIVATIVE; ACYLTRANSFERASE; CARBONYL DERIVATIVE; CARBOXYPEPTIDASE G2; COBALT; DIAMINOPIMELIC ACID; DIMER; GLUTAMIC ACID; HYDROGEN; METAL ION; MONOMER; N ACETYLCITRULLINE DEACETYLASE; OLIGOMER; POLYPEPTIDE; PROTEIN; SELENOMETHIONINE; SUCCINYLDIAMINOPIMELATE DESUCCINYLASE; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; CATALYSIS; CATALYST; CHROMATOGRAPHY; CRYSTAL; CRYSTALLOGRAPHY; DIMERIZATION; DISPERSION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STRUCTURE; HYDROGEN BOND; MODEL; NEISSERIA MENINGITIDIS; NONHUMAN; PLANT DISEASE; POLARIZATION; PRIORITY JOURNAL; PSEUDOMONAS; XANTHOMONAS CAMPESTRIS;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; COBALT; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEISSERIA MENINGITIDIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS;

ARGE; NEISSERIA MENINGITIDIS; PSEUDOMONAS SP.; XANTHOMONAS CAMPESTRIS;

EID: 33846702233     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.05.013     Document Type: Article

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