Mapping the UDP-N-acetylglucosamine regulatory site of human glucosamine-6P synthase by saturation-transfer difference NMR and site-directed mutagenesis

Biochimie

Volumn 97, Issue 1, 2014, Pages 39-48

  Assrir, Nadine ^a   Richez, Celine ^a   Durand, Philippe ^a   Guittet, Eric ^a   Badet, Bernard ^a   Lescop, Ewen ^a   Badet Denisot, Marie Ange ^a  

^a INSTITUT DE CHIMIE DES SUBSTANCES NATURELLES   (France)

Author keywords

Allosteric regulation; Glucosamine 6 phosphate synthase; Glutamine amidotransferase; STD NMR; Transferred NOE; UDPGlcNAc binding site

Indexed keywords

AMINO ACID; FRUCTOSE 6 PHOSPHATE; GLUCOSAMINE; GLUCOSAMINE 6P SYNTHASE; ISOMERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; EUKARYOTIC CELL; NUCLEAR MAGNETIC RESONANCE; SITE DIRECTED MUTAGENESIS; WILD TYPE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA;

ALLOSTERIC REGULATION; D-FRUCTOSE-6-PHOSPHATE; D-GLUCOSAMINE-6-PHOSPHATE; D-GLUCOSE-6-PHOSPHATE; FRU6P; GLC6P; GLCN6P; GLUCOSAMINE-6-PHOSPHATE SYNTHASE; GLUTAMINE AMIDOTRANSFERASE; HGFAT; HUMAN L-GLUTAMINE:D-FRUCTOSE-6P AMIDOTRANSFERASE OR GLUCOSAMINE-6-PHOSPHATE SYNTHASE; NMR; NUCLEAR MAGNETIC RESONANCE; SATURATION TRANSFER DIFFERENCE; STD; STD-NMR; TCEP; TRANSFERRED NOE; TRIS(2-CARBOXYETHYL)PHOSPHINE HYDROCHLORIDE; UDP-N-ACETYL-D-GLUCOSAMINE; UDPGLCNAC; UDPGLCNAC BINDING SITE;

CATALYTIC DOMAIN; ESCHERICHIA COLI; FEEDBACK, PHYSIOLOGICAL; FRUCTOSEPHOSPHATES; GENE EXPRESSION; GLUCOSAMINE; GLUCOSE-6-PHOSPHATE; GLUTAMINE; GLUTAMINE-FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); HUMANS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE;

EID: 84891878087     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2013.09.011     Document Type: Article

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