Abstract
The alpha- and beta-subunits of membrane-bound ATP synthase complex bind ATP and ADP: beta contributes to catalytic sites, and alpha may be involved in regulation of ATP synthase activity. The sequences of beta-subunits are highly conserved in Escherichia coli and bovine mitochondria. Also alpha and beta are weakly homologous to each other throughout most of their amino acid sequences, suggesting that they have common functions in catalysis. Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis, notably myosin, phosphofructokinase, and adenylate kinase, help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP Synthetase Complexes
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Adenosine Diphosphate / metabolism*
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Adenosine Triphosphate / metabolism*
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Adenylate Kinase / metabolism*
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Amino Acid Sequence
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Animals
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Binding Sites
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Cattle
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Escherichia coli / enzymology
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Macromolecular Substances
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Mitochondria, Heart / enzymology
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Mitochondrial ADP, ATP Translocases / metabolism
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Multienzyme Complexes / metabolism*
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Myosins / metabolism*
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Phosphofructokinase-1 / metabolism*
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Phosphotransferases / metabolism*
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Protein Binding
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Rabbits
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Species Specificity
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Submitochondrial Particles / enzymology
Substances
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Macromolecular Substances
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Multienzyme Complexes
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Adenosine Diphosphate
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Adenosine Triphosphate
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Mitochondrial ADP, ATP Translocases
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Phosphotransferases
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Phosphofructokinase-1
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ATP Synthetase Complexes
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Adenylate Kinase
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Myosins