Distinct Modes of Recognition of the Lipoyl Domain as Substrate by the E1 and E3 Components of the Pyruvate Dehydrogenase Multienzyme Complex

Journal of Molecular Biology

Volumn 366, Issue 1, 2007, Pages 132-139

  Fries, Markus ^a   Stott, Katherine M ^a   Reynolds, Stephen ^a   Perham, Richard N ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

lipoyl domain; multienzyme complex; protein protein interaction; pyruvate dehydrogenase; substrate channelling

Indexed keywords

ACYLTRANSFERASE; COCARBOXYLASE; DIHYDROLIPOYL ACETYLTRANSFERASE; MULTIENZYME COMPLEX; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVATE DECARBOXYLASE; PYRUVATE DEHYDROGENASE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOCTIC ACID; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; GENE EXPRESSION; GEOBACILLUS STEAROTHERMOPHILUS; NITROGEN 15 HETERONUCLEAR SINGLE QUANTUM COHERENCE SPECTROSCOPY; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; REDUCTION;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 33846331962     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.018     Document Type: Article

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