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Volumn 424, Issue 1, 2004, Pages 105-111
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Competition between ammonia derived from internal glutamine hydrolysis and hydroxylamine present in the solution for incorporation into UTP as catalysed by Lactococcus lactis CTP synthase
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Author keywords
Allosteric regulation; Glutamate semialdehyde; Half of the sites mechanism; N4 hydroxy CTP; Substrate competition
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Indexed keywords
ADENOSINE DIPHOSPHATE;
ADENOSINE TRIPHOSPHATE;
ALDEHYDE;
AMMONIA;
AMMONIUM CHLORIDE;
CYTIDINE TRIPHOSPHATE;
GLUTAMIC ACID;
GLUTAMINE;
HYDROXIDE;
HYDROXYLAMINE;
NITROGEN;
SYNTHETASE;
URIDINE TRIPHOSPHATE;
ALLOSTERISM;
ARTICLE;
CATALYSIS;
CHEMICAL REACTION;
ENZYME ACTIVATION;
ENZYME ACTIVE SITE;
ENZYME INHIBITION;
HYDROLYSIS;
LACTOCOCCUS LACTIS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
SYNTHESIS;
AMMONIA;
BINDING, COMPETITIVE;
CARBON-NITROGEN LIGASES;
CATALYSIS;
CYTIDINE TRIPHOSPHATE;
ENZYME INHIBITORS;
GLUTAMATES;
GLUTAMINE;
GUANOSINE TRIPHOSPHATE;
HYDROLYSIS;
HYDROXYLAMINE;
KINETICS;
LACTOCOCCUS LACTIS;
PROTEIN BINDING;
PROTEIN SUBUNITS;
SOLUTIONS;
URIDINE TRIPHOSPHATE;
LACTOCOCCUS;
LACTOCOCCUS LACTIS;
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EID: 1542268969
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/j.abb.2004.01.018 Document Type: Article |
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Times cited : (21)
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References (18)
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