- Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis
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Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN-0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 μM and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.
- Ohara-Nemoto, Yuko,Rouf, Shakh M. A.,Naito, Mariko,Yanase, Amie,Tetsuo, Fumi,Ono, Toshio,Kobayakawa, Takeshi,Shimoyama, Yu,Kimura, Shigenobu,Nakayama, Koji,Saiki, Keitarou,Konishi, Kiyoshi,Nemoto, Takayuki K.
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p. 5436 - 5448
(2014/03/21)
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- SOY SAUCE HAVING HYPOTENSIVE EFFECTS AND METHOD FOR PRODUCING THE SAME
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The present invention provides soy sauce that comprises significant amounts of peptides, and, in particular, hypotensive peptide Gly-Tyr and hypotensive peptide Ser-Tyr, exhibiting a high degree of angiotensin-I-converting enzyme-inhibitory activity and has hypotensive effects while containing no hypotensive agent. Target soy sauce is obtained by mixing soy sauce koji having protease activity of 20 to 300 U/g koji with an aqueous common salt solution and subjecting the mixture to heated digestion, followed by compression filtration. Target soy sauce with a good flavor is obtained by adding soy sauce lactic acid bacteria and soy sauce yeast cells to the moromi mash after heated digestion, and subjecting the resultant to fermentation and maturation, followed by compression filtration.
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- TRIMETHYLSILYL CYANIDE IN PEPTIDE STRATEGIES. PART III. NEEDLESSNESS FOR COMPLEMENTARY HYDROXYL SIDE-CHAIN PROTECTION
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No extra side-chain protection is needed for Ser, Thr, Tyr, and Cys (nor for Asp and Glu) in peptide syntheses that are mediated by TMS-CN, whereby silylesters and ethers are formed and are stable enough even during activation of carboxylic components.Thi
- Anteunis, M.J.O.,Becu, Chr.,Becu, F.
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p. 133 - 136
(2007/10/02)
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- EXPERIENCES IN Z-DEPROTECTION. SIMPLE PREPARATIONS OF Z-His and diZ-His.
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A systematic investigation about the possibilities of removing benzyloxycarbonyl groupings in some model peptides acids that resist easy deprotection, have led to some interesting and efficient modified procedures.One-pot synthetic methods for Zα-His-OH and Zα,ZIm-His-OH are also reported.
- Anteunis, M. J. O.,Becu, Chr.,Becu, F.,Reyniers, M.-F.
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p. 775 - 782
(2007/10/02)
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