Evidence of a species-differentiated regulatory domain within the N-terminal region of skeletal muscle AMP deaminase.
Rabbit skeletal muscle AMP deaminase was submitted to limited proteolysis by trypsin that converts the native 80 kDa enzyme subunit to a stable product of approx. 70 kDa, which, in contrast to the native enzyme, is not sensitive to regulation by ATP at pH 6.5. Tryptic peptide mapping indicates that proteolysis is confined to the N-terminal region of the molecule, identifying in this region of AMP deaminase a non-catalytic, 95 residue regulatory domain that stabilises the binding of ATP to a distant site in the molecule. Protein sequence analysis reveals a marked degree of divergence between rat and rabbit skeletal muscle AMP deaminases in the regions containing residues 7-12 and 51-52, giving molecular basis to the hypothesis of the existence of isoenzymes of AMP deaminase in the mature skeletal muscle of the mammals.
Ronca
F
F
Istituto di Chimica Biologica dell'Università di Pisa, Italy.
Ranieri-Raggi
M
M
Brown
P E
PE
Moir
A J
AJ
Raggi
A
A
D000659:AMP Deaminase / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D014357:Trypsin
D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D014357:Trypsin; D000659:AMP Deaminase