Porcine liver aminopeptidase B. Substrate specificity and inhibition by amino acids

Journal of Biochemistry
S KawataS Makisumi

Abstract

Porcine liver aminopeptidase B[EC 3.4.11.6] is highly specific for hydrolysis of beta-naphthylamides of basic L-amino acids; the Km values for L-arginine beta-naphthylamide and L-lysine beta-naphthylamide were 0.035 and 0.12 mM, respectively. The enzyme was inhibited by various alpha-amino acids. Among basic amino acids, L-homoarginine and L-arginine were the most potent inhibitors, L-lysine and L-norarginine (alpha-amino-gamma-guanidinobutyric acid) being less inhibitory. Hydrophobic amino acids also inhibited the enzyme competitively. This suggests that there is a hydrophobic region that binds the side chain of the substrates or inhibitors in the specificity site of the enzyme. Studies on the inhibitions by L-arginine derivatives showed that blocking of the alpha-carboxyl or the alpha-amino group reduced the inhibitory effect of L-arginine. Porcine liver aminopeptidase B was not inhibited by puromycin, whereas bestatin inhibited the enzyme competitively with a Ki value of 1.4 X 10(-8) M. This enzyme had no kinin-converting activity.

Citations

May 24, 2006·Bioscience, Biotechnology, and Biochemistry·Koshiro Migita, Toshihide Nishimura
Jun 15, 2011·Bioscience, Biotechnology, and Biochemistry·Mohammed Alamgir SarkerToshihide Nishimura
Jul 1, 1992·Biological Chemistry Hoppe-Seyler·M Abramić, L Vitale
Sep 12, 2008·Reproduction : the Official Journal of the Society for the Study of Fertility·Camila Eduardo MarinhoPaulo Flavio Silveira
Jan 1, 1983·Archives of Biochemistry and Biophysics·E Söderling

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