Premium
Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold.
Author(s) -
Walker J.E.,
Saraste M.,
Runswick M.J.,
Gay N.J.
Publication year - 1982
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1982.tb01276.x
Subject(s) - walker motifs , biology , atp synthase , atp synthase gamma subunit , enzyme , kinase , biochemistry , nucleotide , beta (programming language) , gene , atpase , atp hydrolysis , computer science , programming language
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.