caa a22 4500 397555601 CHVBK 20180308164801.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021536 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021536 Role of Basic Amino Acids in the Cleavage of Synthetic Peptide Substrates by Mitochondrial Processing Peptidase [Elektronische Daten] [Myeong-Cheol Song, Kunitoshi Shimokata, Sakae Kitada, Tadashi Ogishima, Akio Ito] Our recent experiments using model peptides of rat malate dehydrogenase (MDH) indicated that a proximal arginine and a distal basic amino acid are important for processing by initochondrial processing peptidase (MPP). [Niidome, T., Kitada, S., Shimokata, K., Ogishima, T., and Ito, A. (1994) J. Biol Chem. 269, 24719-24722]. To elucidate If the recognition elements apply to other precursor proteins, we analyzed cleavage of model peptides of human ornithine aminotransferase (OAT). Purified peptidase cleaved peptides that corresponded to N-terminal 1-25 and 3-25 at the correct site (Gly17-Val18 at nearly equal rates. Replacement of Arg16 (−2 position) with lysine or alanine reduced the processing efficiency by 95- and 380-fold, respectively. Either deletion from Met1 to Arg10 or replacement of the basic amino acids between them decreased the processing efficiency considerably. A peptide containing Arg7 in addition to Lys4 and Arg10 was more effective than the control peptide. However, a peptide with one and two consecutive basic amino acids in the distal region had a processing efficiency close to the control peptide. These results indicated that processing of OAT was enhanced by an increase in the number of basic amino acids with a suitable distance between them. In other respects, the processing signal of OAT was essentially the same as that of MDH. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence mitochondrial processing peptidase nationallicence substrate specificity nationallicence Song Myeong-Cheol Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut Shimokata Kunitoshi Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut Kitada Sakae Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut Ogishima Tadashi Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut Ito Akio Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1163-1166 0021-924X 120:6<1163 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021536 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021536 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Song Myeong-Cheol Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut NATIONALLICENCE 700 1- Shimokata Kunitoshi Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut NATIONALLICENCE 700 1- Kitada Sakae Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut NATIONALLICENCE 700 1- Ogishima Tadashi Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut NATIONALLICENCE 700 1- Ito Akio Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-81 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1163-1166 0021-924X 120:6<1163 1996 120 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