Site-specific modification of hemoglobin by methyl acetyl phosphate.
Methyl acetyl phosphate, which was originally synthesized as a site-specific reagent for hydroxybutyrate dehydrogenase [R. Kluger and W.-C. Tsui (1980) J. Org. Chem. 45, 2723], also has an affinity for the binding site for 2,3-diphosphoglycerate in hemoglobin. Three residues in or near this cleft between the beta-chains are acetylated by this reagent, i.e., Val-1, Lys-82, and Lys-144. There is no detectable acetylation of any of the amino groups of the alpha-chain. These results indicate the specificity of methyl acetyl phosphate in its reaction with hemoglobin.
D000107:Acetylation; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000032:analysis; D006801:Humans; D009943:Organophosphorus Compounds / Q000494:pharmacology*; D010746:Phosphonoacetic Acid / Q000031:analogs & derivatives / Q000494:pharmacology*; D010766:Phosphorylation; D014357:Trypsin / Q000494:pharmacology
D000596:Amino Acids; D006454:Hemoglobins; D009943:Organophosphorus Compounds; C014660:methylacetylphosphonate; D014357:Trypsin; D010746:Phosphonoacetic Acid