Substrate specificity of aminopeptidase from the mid-gut gland of the scallop (Patinopecten yessoensis).
An action for various peptides and a kinetic study for amino acid p-nitroanilides (pNAs) and 4-methylcoumaryl-7-amides (MCAs) were performed with purified aminopeptidase from the mid-gut of the scallop. The enzyme preferred dipeptides having Ala, Met, and Phe in the amino-terminal or the penultimate position from the amino-termini. The catalytic efficiencies, k(cat)/K(m) values for Ala-pNA and MCA were the highest in the tested substrates, and those for pNA and MCA substrates having Met or Phe were the next highest. The enzyme was found to be a new alanine-specific aminopeptidase.
Umetsu
Hironori
H
Graduate School of Environmental Science, Aomori University, Kobata, Japan. umetsu@aomori-u.ac.jp
Arai
Mito
M
Ota
Toshinori
T
Abe
Kaoru
K
Uchizawa
Hidemitsu
H
Sasaki
Kazuo
K
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D006868:Hydrolysis; D007422:Intestines / Q000201:enzymology*; D007700:Kinetics; D008974:Mollusca / Q000033:anatomy & histology* / Q000201:enzymology*; D013379:Substrate Specificity
D000626:Aminopeptidases