Title

Classifying glycerol dehydratase by its functional residues and purifying selection in its evolution

Authors

Andres Julian Gutierrez Escobar^1*, Dolly Montoya Castano¹

Affiliation

 ¹Universidad Nacional de Colombia, Bioprocesses and Bioprospecting Research Group, Instituto de Biotecnología Bogotá, Colombia

Email

andresgutierrez@colombia.com; * Corresponding author

Article Type

Hypothesis

Date

Received July 25, 2010; Accepted August 25, 2010; Published October 06, 2010

Abstract

Glycerol dehydratase (GD) catalyses glycerol reductive conversion to 3-hydroxypropanaldehyde (3-HPA), this being the first step required for the microbial conversion of glycerol to 1, 3 -propanodiol. GD has been functionally characterised to date and two main groups have been determined, one of them being vitamin B12-dependent and the other B12-independent. GD evolutionary history has been described and an exhaustive analysis made for detecting the functional residues responsible for type I divergence. GD phylogenetic tree topology was seen to be statistically robust and the data indicated strong purifying selection operating on the GD proteins within it. Two clades were indentified, one for vitamin B12-dependent and the other for B12- independent classes. The ancient hot-pot residues responsible for protein divergency for each clade were also identified. The basic evolutionary biology for GD proteins has been described, thereby opening the way forward for developing rational mutagenesis studies.

Keywords

glycerol dehydratase, molecular evolution, type I functional divergence, hot pots.

Citation

Escobar et al. Bioinformation 5(4): 173-176 (2010)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

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.