Academic Journal

Identification of the Catalytic Triad of Family S46 Exopeptidases, Closely Related to Clan PA Endopeptidases

Bibliographic Details
Title: Identification of the Catalytic Triad of Family S46 Exopeptidases, Closely Related to Clan PA Endopeptidases
Authors: Suzuki, Yoshiyuki, Sakamoto, Yasumitsu, Tanaka, Nobutada, Okada, Hirofumi, Morikawa, Yasushi, Ogasawara, Wataru
Publisher Information: Nature Publishing Group
Publication Year: 2014
Collection: PubMed Central (PMC)
Subject Terms: Article
Description: The exopeptidases of family S46 are exceptional, as the closest homologs of these enzymes are the endopeptidases of clan PA. The three-dimensional structure of S46 enzymes is unknown and only one of the catalytic residues, the serine, has been identified. The catalytic histidine and aspartate residues are not experimentally identified. Here we present phylogenetic and experimental data that identify all residues of the catalytic triad of S46 peptidase, dipeptidyl aminopeptidase BII (DAP BII) from Pseudoxanthomonas mexicana WO24. Phylogenetic comparison with the protein and S46 peptidases, revealed His-86, Ser-657, and five aspartate residues as possible catalytic residues. Mutation studies identified the catalytic triad of DAP BII as His-86, Asp-224, and Ser-657, while secondary structure analysis predicted an extended alpha-helical domain in between Asp-224 and Ser-657. This domain is unique for family S46 exopeptidases and its absence from the endopeptidases of clan PA might be key to their different hydrolysis activities.
Document Type: text
Language: English
Relation: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944710; http://www.ncbi.nlm.nih.gov/pubmed/24598890; http://dx.doi.org/10.1038/srep04292
DOI: 10.1038/srep04292
Availability: https://doi.org/10.1038/srep04292
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944710
http://www.ncbi.nlm.nih.gov/pubmed/24598890
Rights: Copyright © 2014, Macmillan Publishers Limited. All rights reserved ; http://creativecommons.org/licenses/by-nc-nd/3.0/ ; This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/
Accession Number: edsbas.175EB374
Database: BASE
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