title: The complete amino acid sequence of adenylate kinase from baker's yeast.
abstract: The complete amino acid sequence of cytosolic adenylate kinase (MgATP + AMP----MgADP + ADP) from baker's yeast has been determined. Tryptic and clostripaic cleavage of the protein yielded 27 and 10 fragments, respectively. They were sequenced with either a solid-phase sequencer or a gas-phase sequencer. Alignment of the clostripaic fragments was deduced from the sequence of peptides obtained by endoproteinase Lys-C and cyanogen bromide cleavages. The N-terminus is blocked by an acetyl group as shown by proton magnetic resonance. Carboxypeptidase A digestion of the whole protein showed that the C-terminal sequence is -Lys-Asn, in agreement with the sequence of peptides from tryptic, clostripaic and 2-iodosobenzoic acid cleavages. The enzyme is a monomer of 220 amino acids with Mr 24077. Comparison of the sequence of the cytosolic adenylate kinases from yeast and pig shows 25% identity with highly conserved segments in the putative active-site region of the enzyme. After position 111, however, there is an insertion of 32 residues in the yeast species, similar to the adenylate kinase and the GTP:AMP phosphotransferase from beef heart mitochondria.
mesh_terms: D000263:Adenylate Kinase / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D003600:Cytosol / Q000201:enzymology; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D010770:Phosphotransferases / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D010770:Phosphotransferases; D000263:Adenylate Kinase; D010447:Peptide Hydrolases