title: Investigation of myosin substrate-binding site using phosphorylating analogs of the substrate.
abstract: Affinity modification of HMM has been performed, using mixed anhydrides of AMP, epsilon AMP, ADP or IMP and sterically hindered aromatic carbonic acids. The affinity labelling site of HMM was demonstrated to be highly specific towards the adenosine fragment of the affinity analog. The number of phosphate groups and the hydrophobicity of the aromatic acid substitutents did not influence the mode of the analogs interaction with HMM. The data obtained confirms our previous suggestion that the nucleotide analogs in question modify the substrate binding site which is other than the active site of the enzyme.
authors.forename: V M
authors.initials: VM
authors.lastname: Kodentsova
authors.forename: E V
authors.initials: EV
authors.lastname: Petushkova
authors.forename: S S
authors.initials: SS
authors.lastname: Tretyakova
authors.forename: N I
authors.initials: NI
authors.lastname: Sokolova
authors.forename: Z A
authors.initials: ZA
authors.lastname: Shabarova
mesh_terms: D000227:Adenine Nucleotides / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors; D007291:Inosine Monophosphate / Q000378:metabolism; D007700:Kinetics; D015879:Myosin Subfragments / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D013329:Structure-Activity Relationship
chemical_list: D000227:Adenine Nucleotides; D015879:Myosin Subfragments; D007291:Inosine Monophosphate; D009218:Myosins; D000252:Calcium-Transporting ATPases