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An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus

View at Publisher Website:http://www.jbb.uni-plovdiv.bg/documents/27807/352484/jbb_2014-3%281%29-pages_49-60.pdf. This is an open-access journal distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives license (http://creativecommons.org/licenses/by-nc-nd/3.0/).

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Bibliographic Details
Main Authors: Simon Brown, Noorzaid Muhamad, Lisa R. Walker, Kevin C. Pedley, David C. Simcock, (UniKL RCMP)
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Published: University of Plovdiv 2015
Subjects:
glutamate dehydrogenase
structure
Teladorsagia circumcincta
parasite
nematode
Online Access:http://localhost/xmlui/handle/123456789/10243
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spelling my.unikl.ir-102432015-06-17T08:56:11Z An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus Simon Brown Noorzaid Muhamad Lisa R. Walker Kevin C. Pedley David C. Simcock (UniKL RCMP) glutamate dehydrogenase structure Teladorsagia circumcincta parasite nematode View at Publisher Website:http://www.jbb.uni-plovdiv.bg/documents/27807/352484/jbb_2014-3%281%29-pages_49-60.pdf. This is an open-access journal distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives license (http://creativecommons.org/licenses/by-nc-nd/3.0/). Nematode glutamate dehydrogenase (GDH) amino acid sequences are very highly conserved (68-99% identity) and are also very similar to those of the bovine and human enzymes (54-60% identity). The residues involved in binding nucleotides or substrates are completely conserved and tend to be located in highly conserved regions of the sequence. Based on the strong homology between the bovine, Teladorsagia circumcincta and Haemonchus contortus GDH sequences, models of the structure of the T. circumcincta and H. contortus monomers were constructed. The structure of the T. circumcincta monomer obtained using SWISS-MODEL was very similar to that of the bovine enzyme monomer and the backbone of the polypetide deviated very little from that of the bovine enzyme monomer. Despite the sequence differences between the bovine and T. circumcincta enzymes, the relative positions and orientations of the residues involved in ligand binding were very similar. The reported Km for NADP+ of T. circumcincta is about 35 and times that of the bovine enzyme, whereas the Kms of the two enzymes for glutamate, α-ketoglutarate and NAD(P)H are much more similar. The residue corresponding to S267 of the bovine enzyme is involved in binding the 2'-phosphate of NADP+ and is replaced in the T. circumcincta and H. contortus sequences by a tryptophan. The partial occlusion of the NAD(P)-binding site by the tryptophan sidechain and the loss of at least one potential H-bond provided by the serine may explain the lower affinity of the T. circumcincta for NADP+ 2015-06-17T08:54:14Z 2015-06-17T08:54:14Z 2014 Brown, Simon, Muhamad, Noorzaid, Walker, Lisa R., Pedley, Kevin C., and Simcock, David C. (2014) An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus. Journal of Bioscience and Biotechnology, 3 (1). pp. 49-60. http://localhost/xmlui/handle/123456789/10243 University of Plovdiv
institution Universiti Kuala Lumpur
building UniKL Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Kuala Lumpur
content_source UniKL Institutional Repository
url_provider http://ir.unikl.edu.my/
topic glutamate dehydrogenase
structure
Teladorsagia circumcincta
parasite
nematode
spellingShingle glutamate dehydrogenase
structure
Teladorsagia circumcincta
parasite
nematode
Simon Brown
Noorzaid Muhamad
Lisa R. Walker
Kevin C. Pedley
David C. Simcock
(UniKL RCMP)
An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus
description View at Publisher Website:http://www.jbb.uni-plovdiv.bg/documents/27807/352484/jbb_2014-3%281%29-pages_49-60.pdf. This is an open-access journal distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
format
author Simon Brown
Noorzaid Muhamad
Lisa R. Walker
Kevin C. Pedley
David C. Simcock
(UniKL RCMP)
author_facet Simon Brown
Noorzaid Muhamad
Lisa R. Walker
Kevin C. Pedley
David C. Simcock
(UniKL RCMP)
author_sort Simon Brown
title An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus
title_short An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus
title_full An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus
title_fullStr An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus
title_full_unstemmed An in silico analysis of the glutamate dehydrogenases of Teladorsagia circumcincta and Haemonchus contortus
title_sort in silico analysis of the glutamate dehydrogenases of teladorsagia circumcincta and haemonchus contortus
publisher University of Plovdiv
publishDate 2015
url http://localhost/xmlui/handle/123456789/10243
_version_ 1644485106275975168
score 13.160551

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