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...
Main Authors: | , , , , |
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Format: | Article |
Language: | English |
Published: |
Plovdiv University Press
2014-04-01
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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/ |