Amino acid sequence and three-dimensional structure of cytosolic adenylate kinase from carp muscle.
The amino acid sequence of cytosolic adenylate kinase from carp muscle has been determined. For the analysis of the blocked amino terminus an N-acylaminoacyl peptidase has been isolated and applied successfully. The resulting sequence is homologous to those of other adenylate kinases. It has 76% and 74% identical amino acids when compared with the enzymes from chicken and pig, respectively. The carp enzyme forms X-ray-grade crystals, the structure of which has been solved at 0.58-nm resolution. The observed chain fold is very similar to the known fold of the porcine enzyme in crystal form-A, whereas the molecular packing arrangements are quite different. This finding confirms that the observed porcine enzyme structure is intrinsically stable and has not been enforced during the crystallization process. The sequence of cytosolic adenylate kinase from carp muscle is: (table; see text)
Reuner
C
C
Institut für Organische Chemie und Biochemie der Universität, Freiburg, Federal Republic of Germany.
Hable
M
M
Wilmanns
M
M
Kiefer
E
E
Schiltz
E
E
Schulz
G E
GE
D000263:Adenylate Kinase / Q000235:genetics / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000818:Animals; D002347:Carps; D003600:Cytosol / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D010770:Phosphotransferases / Q000235:genetics; D011487:Protein Conformation
D010446:Peptide Fragments; D010770:Phosphotransferases; D000263:Adenylate Kinase; D010447:Peptide Hydrolases