The primary structure of chicken muscle acylphosphatase isozyme Ch2.
The amino acid sequence of one, Ch2, of the two isozymes of chicken muscle acylphosphatase was determined. It consists of 98 amino acid residues with N-acetylalanine at the amino(N)-terminus and contains no cysteine: Ac-Ala-Gly-Ser-Glu- Gly-Leu-Met-Ser-Val-Asp-Tyr-Glu-Val-Ser-Gly-Arg-Val-Gln-Gly-Val-Phe-Phe- Arg- Lys-Tyr-Thr-Gln-Ser-Glu-Ala-Lys-Arg-Leu-Gly-Leu-Val-Gly-Trp-Val-Arg-Asn- Thr- Ser-His-Gly-Thr-Val-Gln-Gly-Gln-Ala-Gln-Gly-Pro-Ala-Ala-Arg-Val-Arg-Glu- Leu- Gln-Glu-Trp-Leu-Arg-Lys-Ile-Gly-Ser-Pro-Gln-Ser-Arg-Ile-Ser-Arg-Ala-Glu- Phe- Thr-Asn-Glu-Lys-Glu-Ile-Ala-Ala-Leu-Glu-His-Thr-Asp-Phe-Gln-Ile-Arg-Lys- COOH. The sequence differs in 44% of the total positions from the other isozyme, Ch1. Comparison of the sequence and the predicted conformational profile of Ch2 with those of Ch1 suggests that they share a common evolutionary origin and appear to have retained similar conformations throughout their evolutionary development.
Ohba
Y
Y
Institute of Immunological Science, Hokkaido University.
Minowa
O
O
Mizuno
Y
Y
Shiokawa
H
H
D017766:Acid Anhydride Hydrolases; D000421:Alcaligenes / Q000201:enzymology; D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002645:Chickens; D003488:Cyanogen Bromide; D007527:Isoenzymes; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D010744:Phosphoric Monoester Hydrolases; D011487:Protein Conformation; D012697:Serine Endopeptidases; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D003488:Cyanogen Bromide; D007527:Isoenzymes; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D010744:Phosphoric Monoester Hydrolases; D012697:Serine Endopeptidases; D000097024:Acylphosphatase; C038220:acylaminoacyl-peptidase; C028344:glutamyl endopeptidase; C036813:lysyl endopeptidase