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

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...

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Bibliographic Details
Main Authors: SIMON BROWN, NOORZAID MUHAMAD, LISA R. WALKER, KEVIN C. PEDLEY, DAVID C. SIMCOCK
Format: Article
Language:English
Published: Plovdiv University Press 2014-04-01
Series:Journal of BioScience and Biotechnology
Subjects:
Online Access:http://www.jbb.uni-plovdiv.bg/documents/27807/352484/jbb_2014-3(1)-pages_49-60.pdf/