PMID:8747466
| Citation |
Athappilly, FK and Hendrickson, WA (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3:1407-19 |
|---|---|
| Abstract |
Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. Universally, this reaction involves three functional components all related to a carboxybiotinyl intermediate. A biotinyl domain shuttles its covalently attached biotin prosthetic group between the active sites of a biotin carboxylase and a carboxyl transferase. In Escherichia coli, the three components reside in separate subunits: a biotinyl domain is the functional portion of one of these, biotin carboxy carrier protein (BCCP). |
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| Keywords |
Acetyl-CoA Carboxylase/chemistry; Acetyl-CoA Carboxylase/metabolism; Amino Acid Oxidoreductases/chemistry; Amino Acid Sequence; Bacterial Proteins/chemistry; Binding Sites; Biotin/chemistry; Biotin/metabolism; Crystallography, X-Ray/methods; Escherichia coli/enzymology; Evolution, Molecular; Geobacillus stearothermophilus/enzymology; Glycine Dehydrogenase (Decarboxylating); Humans; Hydrogen Bonding; Lysine/analogs & derivatives; Lysine/chemistry; Lysine/metabolism; Models, Molecular; Molecular Sequence Data; Multiple Carboxylase Deficiency/enzymology; Peptide Fragments/chemistry; Plant Proteins/chemistry; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Pyruvate Dehydrogenase Complex/chemistry; Recombinant Fusion Proteins/chemistry; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Structure-Activity Relationship |
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