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Title
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The complete amino acid sequence of adenylate kinase from baker's yeast.
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Authors
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A.G.Tomasselli,
E.Mast,
W.Janes,
E.Schiltz.
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Ref.
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Eur J Biochem, 1986,
155,
111-119.
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PubMed id
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Abstract
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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.
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