Crystal Structure of the N-Acetyltransferase Domain of Human N-Acetyl-L-Glutamate Synthase in Complex with N-Acetyl-L-Glutamate Provides Insights into Its Catalytic and Regulatory Mechanisms

PLoS ONE

Volumn 8, Issue 7, 2013, Pages

  Zhao, Gengxiang ^a   Jin, Zhongmin ^b   Allewell, Norma M ^c   Tuchman, Mendel ^a   Shi, Dashuang ^a  

^a GEORGE WASHINGTON UNIVERSITY   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

^c University of Maryland   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID KINASE; ARGININE; CARBAMOYL PHOSPHATE SYNTHASE; DEANOL ACEGLUMATE; GLUTAMATE ACETYLTRANSFERASE; PHOSPHOTRANSFERASE; PROLINE RICH PROTEIN; UNCLASSIFIED DRUG;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; GEL FILTRATION; HUMAN; NONHUMAN; OLIGOMERIZATION; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 84880839974     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0070369     Document Type: Article

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