Pazzagli L, Manao G, Cappugi G, Caselli A, Camici G, Moneti G, Ramponi G
Dipartimento di Scienze Biochimiche, Università di Firenze, Viale Morgagni 50, I-50134 Florence, Italy.
Biochim Biophys Acta. 1998 Sep 8;1387(1-2):264-74. doi: 10.1016/s0167-4838(98)00134-4.
Two acylphosphatase isoenzymes have been purified from Lamna nasus muscle, and their complete amino acid sequences have been determined. The former (E1) consists of 99 amino acid residues, while the latter (E2) consists of 102 residues. Both are acetylated at their N termini. E1 has the FFRK active site motif characteristic of all common-type acylphosphatase isoenzymes, whereas E2 contains the CFRM active site motif characteristic of all muscle-type acylphosphatase isoenzymes. They have quite similar kinetic properties. The comparison of sequences of fish E1 and E2 isoenzymes with other known mammalian and bird acylphosphatases reveals that the E2 isoenzyme has an N terminus tail, four residues long, similar to those previously found in all known bird species muscle-type isoenzymes. Among organ-common-type acylphosphatases about 50% of residues are completely conserved, whereas about 60% of muscle-type acylphosphatase residues are completely conserved, indicating that the latter type of isoenzyme has a slower evolutionary rate than the former. The sequences of E1 and E2 acylphosphatases from L. nasus represent the first primary structures of this kind of enzyme determined among fish species.
