The Primary Structure of Chicken Muscle Acylphosphatase Isozyme Ch1

• Published in: Journal of biochemistry (Tokyo) Vol. 102; no. 5; pp. 1213 - 1220
• Main Authors: MINOWA, Osamu, OHBA, Yoichi, MIZUNO, Yusuke, SHIOKAWA, Hiroyuki
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01.11.1987
• Subjects: Acid Anhydride Hydrolases; Acylphosphatase; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chickens; Chymotrypsin; Cyanogen Bromide; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; Isoenzymes; Metalloendopeptidases; Molecular Sequence Data; Muscles - enzymology; Peptide Fragments; Phosphoric Monoester Hydrolases; Sequence Homology, Nucleic Acid; Trypsin; Enzyme; Isozyme; Acylphosphatase; Interspecific comparison; Primary structure; Vertebrata; Mammalia; Muscle; Chicken; Intraspecific comparison; Aves; Comparative study; Aminoacid sequence
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a122160

The amino acid sequence of chicken muscle acylphosphatase isozyme Ch1 was determined. The protein consists of 102 amino acid residues, does not contain histidine, and the NH2-terminus is acetylated: Ac-Ser-Ala-Leu-Thr-Lys-Ala-Ser-Gly-Ser-Leu-Lys-Ser-Val-Asp-Tyr-Glu-Val-Phe-Gly-Arg-Val-Gln-Gly-Val-Cys-Phe-Arg-Met-Tyr-Thr-Glu-Glu-Glu-Ala-Arg-Lys-Leu-Gly-Val-Val-Gly-Trp-Val-Lys-Asn-Thr-Ser-Gln-Gly-Thr-Val-Thr-Gly-Gln-Val-Gln-Gly-Pro-Glu-Asp-Lys-Val-Asn-Ala-Met-Lys-Ser-Trp-Leu-Ser-Lys-Val-Gly-Ser-Pro-Ser-Ser-Arg-Ile-Asp-Arg-Thr-Lys-Phe-Ser-Asn-GIu-Lys-Glu-Ile-Ser-Lys-Leu-Asp-Phe-Ser-Gly-Phe-Ser-Thr-Arg-Tyr-OH. This sequence differs in 44% of the total positions from the other isozyme (Ch2) of chicken muscle acylphosphatase (Ohba et al., the accompanying paper). The sequence of Ch1 has three substitutions from that of turkey muscle acylphosphatase; these are Ser from Ala at position 9, Ser from Arg at 47, and Lys from Asn at 83. The sequence has about 80% homology with those of mammalian muscle acylphosphatases.