Identification of ADP in the iron-sulfur flavoprotein trimethylamine dehydrogenase.
作者： L W Lim , F S Mathews , D J Steenkamp
DOI: 10.1016/S0021-9258(18)69036-2
关键词: Amino acid 、 Binding site 、 Stereochemistry 、 NADPH binding 、 Trimethylamine dehydrogenase 、 Flavoprotein 、 Biochemistry 、 Chemistry 、 Moiety 、 Cofactor 、 Protein subunit
摘要: Abstract Analysis of the 2.4-A resolution electron density map trimethylamine dehydrogenase has revealed unexpected presence one molecule ADP/subunit. This binding been confirmed chemically. The site is located at analogous position ADP moiety FAD in glutathione reductase, and NADPH domains which resemble two dehydrogenase. Comparison environments moieties proteins indicates that 32 residues 6 peptides are equivalent positions with a root mean square deviation for C alpha 1.11 A. Twelve these amino acids identical, based on density-derived "x-ray" sequence Detailed analysis environment most conserved not direct contact cofactor. Some them probably represent "fingerprint" beta fold found dinucleotide proteins, but remaining may indicate closer evolutionary relationship between proteins.
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