The active site and substrates binding mode of malonyl-CoA synthetase determined by transferred nuclear Overhauser effect spectroscopy, site- directed mutagenesis, and comparative modeling studies

Protein Science

Volumn 9, Issue 7, 2000, Pages 1294-1303

  Jung, Jin Won ^a   An, Jae Hyung ^a   Na, Kyu Bong ^a   Kim, Yu Sam ^a   Lee, Weontae ^a  

^a Yonsei University   (South Korea)

Author keywords

Adenylate forming enzyme; Malonyl CoA; Malonyl CoA synthetase; Molecular modeling; NMR

Indexed keywords

MALONYL COENZYME A; SYNTHETASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN FOLDING; RHIZOBIUM TRIFOLII; SITE DIRECTED MUTAGENESIS;

EID: 0343193205     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1294     Document Type: Article

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