Title |
Characterization of TPP-binding proteins in Methanococci archaeal species
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Authors |
Laura K. Harris1,2*
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Affiliation |
1Department of Science, Davenport University, Lansing, Michigan, United States of America; 2Department of Health Informatics, Rutgers School of Health Professions, Newark, New Jersey, United States of America
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Laura K. Harris - E-mail: laura.harris@davenport.edu; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received August 22, 2016; Accepted November 5, 2016; Published November 22, 2016
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Abstract |
Acetolactate synthase (ALS) is a
highly conserved protein family responsible for producing branched
chain amino acids. In Methanocaldococcus jannaschii, two ALS
proteins, MJ0277 and MJ0663 exist though variations in features
between them are noted. Researchers are quick to examine MJ0277
homologs due to their increased function and close relationship, but
few have characterized MJ0663 homologs. This study identified
homologs for both MJ0277 and MJ0663 in all 15 Methanococci species
with fully sequenced genomes. EggNOG database does not define four
of the MJ0663 homologs, JH146_1236, WP_004591614, WP_018154400, and
EHP89635. BLASTP comparisons suggest these four proteins had around
30% identity to MJ0277 homologs, close to the identity similarities
between other MJ0663 homologs to the MJ0277 homologous group. ExPASY
physiochemical characterization shows a statistically significant
difference in molecular weight and grand average hydropathy between
homologous groups. CDD-BLAST showed distinct domains
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Keywords: |
TPP-binding, proteins, Methanococci, archaeal, species
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Citation |
Harris, Bioinformation 12(8) 359-367 (2016)
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Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
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