Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase

Burkholderia pseudomallei K96243, the causative agent of melioidosis, is reported to produce various extracellular products, including proteases. The role of these proteases in the melioidosis, however, remains obscure. Previous findings have hinted at the inherent pathogenicity of the protease duri...

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Main Authors:	Azizan, Muhammad Talhah, Muhamad Bunnori, Noraslinda
Format:	Conference or Workshop Item
Language:	English
Published:	2014
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/40023/ http://irep.iium.edu.my/40023/1/5th._Malaysian_Symposium_of_Biomedical_Science_Noraslinda.pdf

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recordtype	eprints
spelling	iium-400232018-06-19T07:13:10Z http://irep.iium.edu.my/40023/ Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase Azizan, Muhammad Talhah Muhamad Bunnori, Noraslinda TP248.13 Biotechnology Burkholderia pseudomallei K96243, the causative agent of melioidosis, is reported to produce various extracellular products, including proteases. The role of these proteases in the melioidosis, however, remains obscure. Previous findings have hinted at the inherent pathogenicity of the protease during B. pseudomallei K96243 infection. The annotated sequences by Wellcome Trust Sanger for the two families of metallopeptidases and serine peptidase are not full annotated.We chose to annotate the two major families peptidases, i.e. serine peptidases and metallopeptidases present in B. pseudomallei K96243. A total of 3065 non-redundant query sequences of characterized and predicted proteases were obtained and predicted proteases were obtained by using text searched and from a few databases (NCBI, MEROPS, BRENDA and UniProtKB). The redundant sequences will be omitted by using ARTEMIS tools. The BLASTP searched against B. pseudomallei K96243 genome and conserved domains/motifs were identified by searching InterPro database. The multiple sequence alignments and active sites are annotated by using ClustalX with known sequences from other organisms and the consequences were deduced by the BOXSHADE. There was only hydrolases classes (EC3) have been distinguished from a total eighty identified peptidases and comprised two type of compound/group involved which are EC3.5 (carbon-nitrogen bond) and EC3.4 (peptide bond). Only a peptidase from S45 family has predicted belongs to EC3.5 and the rest of 79 peptidases are hydrolases acting on peptide bond. There are seven groups specified based on the nature of reaction: EC3.4.11 (aminopeptidases), EC3.4.13 (dipeptidases), EC3.4.14 (dipeptidyl and tripeptidyl-peptidases), EC3.4.16 (serine-type carboxypeptidase), EC3.4.17 (metallo-type carboxypeptidases), EC3.4.21 (serine endopeptidases) and EC3.4.24 (metalloproteases) and each group comprised 30.8%, 3.8%, 2.6%, 12.7%, 1.3%, 27% and 20.5% respectively. Although EC3.4.11 has the highest percentage of peptidases but the group consists both serine and metallopeptidase unlike EC3.4.21 and EC3.4.24 which only have either serine or metallopeptidases.In this study, we have characterized 48 serine peptidases and 32 metallopeptidases based on their functional domains and active sites by making comparisons with known peptidase functions. The collection of 80 peptidases has been characterized based on EC group. The group of the peptide bond (EC3.4) accumulated about 98% of the total peptidase that has annotated. The classification for both serine and metallopeptidases to the peptidase family facilitate identifying the potential peptidases which contribute as virulence factors. 2014-05-10 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/40023/1/5th._Malaysian_Symposium_of_Biomedical_Science_Noraslinda.pdf Azizan, Muhammad Talhah and Muhamad Bunnori, Noraslinda (2014) Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase. In: 5th Malaysian Symposium of Biomedical Science, 10th-11th May 2014, Kuala Lumpur. (Unpublished)
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Azizan, Muhammad Talhah Muhamad Bunnori, Noraslinda Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase
description	Burkholderia pseudomallei K96243, the causative agent of melioidosis, is reported to produce various extracellular products, including proteases. The role of these proteases in the melioidosis, however, remains obscure. Previous findings have hinted at the inherent pathogenicity of the protease during B. pseudomallei K96243 infection. The annotated sequences by Wellcome Trust Sanger for the two families of metallopeptidases and serine peptidase are not full annotated.We chose to annotate the two major families peptidases, i.e. serine peptidases and metallopeptidases present in B. pseudomallei K96243. A total of 3065 non-redundant query sequences of characterized and predicted proteases were obtained and predicted proteases were obtained by using text searched and from a few databases (NCBI, MEROPS, BRENDA and UniProtKB). The redundant sequences will be omitted by using ARTEMIS tools. The BLASTP searched against B. pseudomallei K96243 genome and conserved domains/motifs were identified by searching InterPro database. The multiple sequence alignments and active sites are annotated by using ClustalX with known sequences from other organisms and the consequences were deduced by the BOXSHADE. There was only hydrolases classes (EC3) have been distinguished from a total eighty identified peptidases and comprised two type of compound/group involved which are EC3.5 (carbon-nitrogen bond) and EC3.4 (peptide bond). Only a peptidase from S45 family has predicted belongs to EC3.5 and the rest of 79 peptidases are hydrolases acting on peptide bond. There are seven groups specified based on the nature of reaction: EC3.4.11 (aminopeptidases), EC3.4.13 (dipeptidases), EC3.4.14 (dipeptidyl and tripeptidyl-peptidases), EC3.4.16 (serine-type carboxypeptidase), EC3.4.17 (metallo-type carboxypeptidases), EC3.4.21 (serine endopeptidases) and EC3.4.24 (metalloproteases) and each group comprised 30.8%, 3.8%, 2.6%, 12.7%, 1.3%, 27% and 20.5% respectively. Although EC3.4.11 has the highest percentage of peptidases but the group consists both serine and metallopeptidase unlike EC3.4.21 and EC3.4.24 which only have either serine or metallopeptidases.In this study, we have characterized 48 serine peptidases and 32 metallopeptidases based on their functional domains and active sites by making comparisons with known peptidase functions. The collection of 80 peptidases has been characterized based on EC group. The group of the peptide bond (EC3.4) accumulated about 98% of the total peptidase that has annotated. The classification for both serine and metallopeptidases to the peptidase family facilitate identifying the potential peptidases which contribute as virulence factors.
format	Conference or Workshop Item
author	Azizan, Muhammad Talhah Muhamad Bunnori, Noraslinda
author_facet	Azizan, Muhammad Talhah Muhamad Bunnori, Noraslinda
author_sort	Azizan, Muhammad Talhah
title	Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase
title_short	Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase
title_full	Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase
title_fullStr	Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase
title_full_unstemmed	Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase
title_sort	identification and characterization of burkholderia pseudomallei k96243 serine and metallopeptidase
publishDate	2014
url	http://irep.iium.edu.my/40023/ http://irep.iium.edu.my/40023/1/5th._Malaysian_Symposium_of_Biomedical_Science_Noraslinda.pdf
first_indexed	2023-09-18T20:57:27Z
last_indexed	2023-09-18T20:57:27Z
_version_	1777410398825218048

Identification and characterization of burkholderia pseudomallei K96243 serine and metallopeptidase

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