Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit

Biochemistry

Volumn 43, Issue 44, 2004, Pages 14037-14046

  Park, Yun Hee ^a   Wei, Wen ^a   Zhou, Leon ^a   Nemeria, Natalia ^a   Jordan, Frank ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CARBOXYLATION; DIMERS; ENZYMES; ESCHERICHIA COLI; SPECTROSCOPIC ANALYSIS; SUBSTITUTION REACTIONS;

AMINO TERMINAL RESIDUES; DECARBOXYLATION; DEHYDROGENASE;

AMINO ACIDS;

COCARBOXYLASE; PYRUVATE DEHYDROGENASE COMPLEX; PYRUVATE DEHYDROGENASE COMPLEX E1; PYRUVATE DEHYDROGENASE COMPLEX E2; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

ACETYLATION; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; DECARBOXYLATION; DIMERIZATION; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; MASS SPECTROMETRY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN INTERACTION; REDUCTION; SEQUENCE ALIGNMENT;

ACETYLATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE; DIMERIZATION; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; HEAT; HYDROLYSIS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PYRUVATE DEHYDROGENASE (LIPOAMIDE); PYRUVATE DEHYDROGENASE COMPLEX; SEQUENCE DELETION; THIOCTIC ACID; TRYPSIN; VARIATION (GENETICS);

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; NEGIBACTERIA;

EID: 8344289722     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049027b     Document Type: Article

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