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Volumn 284, Issue 8, 2009, Pages 4873-4880
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Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase by L-arginine
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Author keywords
[No Author keywords available]
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Indexed keywords
ACTIVE SITE;
ALLOSTERIC INHIBITION;
BOUND LIGANDS;
CONFORMATIONAL CHANGE;
FEEDBACK INHIBITION;
HEXAMER;
IN-PLANT;
INTER-DOMAIN;
KINASE ACTIVITY;
L-ARGININE;
L-GLUTAMATE;
LOCAL MOTIONS;
N-ACETYLTRANSFERASE;
NEISSERIA GONORRHOEAE;
SPECIFIC ACTIVITY;
SYNTHASE;
TWO DOMAINS;
AMINES;
BINDING ENERGY;
BINDING SITES;
BIOCHEMICAL ENGINEERING;
BIOCHEMISTRY;
ENZYMES;
OLIGOMERS;
ORGANIC ACIDS;
POSITIVE IONS;
AMINO ACIDS;
ACYLTRANSFERASE;
AMINO ACID KINASE;
ARGININE;
COENZYME A;
GLUTAMATE ACETYLTRANSFERASE;
GLUTAMIC ACID;
MONOMER;
PHOSPHOTRANSFERASE;
UNCLASSIFIED DRUG;
AMINO ACID ACETYLTRANSFERASE;
BACTERIAL PROTEIN;
ALLOSTERISM;
AMINO ACID SEQUENCE;
ARTICLE;
BINDING SITE;
COMPLEX FORMATION;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
CRYSTALLIZATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME INHIBITION;
ENZYME SUBUNIT;
LIGAND BINDING;
NEISSERIA GONORRHOEAE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN DOMAIN;
SEQUENCE ANALYSIS;
CHEMISTRY;
COMPARATIVE STUDY;
DIMERIZATION;
DRUG ANTAGONISM;
ENZYMOLOGY;
METABOLISM;
PHYSIOLOGY;
PROTEIN QUATERNARY STRUCTURE;
PROTEIN SECONDARY STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
STRUCTURAL HOMOLOGY;
X RAY CRYSTALLOGRAPHY;
NEISSERIA GONORRHOEAE;
ALLOSTERIC REGULATION;
AMINO-ACID N-ACETYLTRANSFERASE;
ARGININE;
BACTERIAL PROTEINS;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
NEISSERIA GONORRHOEAE;
PROTEIN STRUCTURE, QUATERNARY;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
STRUCTURAL HOMOLOGY, PROTEIN;
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EID: 64149093545
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M805348200 Document Type: Article |
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Times cited : (24)
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References (31)
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