caa a22 4500 397558244 CHVBK 20180308164809.0 cr unu---uuuuu 161202e199603 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021265 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021265 Prolyl Aminopeptidase Is Also Present in Enterobacteriaceae: Cloning and Sequencing of the Hafnia alvei Enzyme-Gene and Characterization of the Expressed Enzyme [Elektronische Daten] [Ana Kitazono, Atsuko Kitano, Tsutomu Kabashima, Kiyoshi Ito, Tadashi Yoshimoto] The Hafnia alvei prolyl aminopeptidase gene (hpap) was cloned and sequenced, the expressed enzyme (HPAP) was purified to homogeneity and thoroughly characterized.An open reading frame of 1,281 bp was found to code for the enzyme, resulting in a protein of 427 amino acids with a molecular weight of 48,577. HPAP resembles the Aeromonas sobria enzyme, having 45% identity and the same distinctive properties with respect to size and substrate specificities. Both enzymes show similar chromatographic behavior, and HPAP could be purified following the procedure previously described for the Aeromonas enzyme. HPAP was found to be resistant to diisopropylphosphofluoridate as are most of the prolyl aminopeptidases hitherto described. In spite of this similarity, no inhibition by 1 mM p-chloromercuribenzoate solution could be detected. Significant inhibition was, however, observed when the enzyme was incubated with 3,4-dichloroisocoumarin. This study confirms the presence of two types of prolyl aminopeptidases, of which the Hafnia and Aeromonas enzymes constitute one group and the Bacillus, Neisseria, and Lactobacillus enzymes the other, and describes the cloning of the first prolyl aminopeptidase gene from an Enterobacteriaceae. © by the Journal of Biochemistry Regular Papers nationallicence aminopeptidase nationallicence Hafnia alvei nationallicence iminopeptidase nationallicence proline nationallicence Kitazono Ana School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut Kitano Atsuko School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut Kabashima Tsutomu School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut Ito Kiyoshi School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut Yoshimoto Tadashi School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut The Journal of Biochemistry Oxford University Press 119/3(1996-03), 468-474 0021-924X 119:3<468 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021265 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021265 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kitazono Ana School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut NATIONALLICENCE 700 1- Kitano Atsuko School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut NATIONALLICENCE 700 1- Kabashima Tsutomu School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut NATIONALLICENCE 700 1- Ito Kiyoshi School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut NATIONALLICENCE 700 1- Yoshimoto Tadashi School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, Nagasaki 852 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/3(1996-03), 468-474 0021-924X 119:3<468 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford