Deciphering the catalytic amino acid residues of l -2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1: An in silico analysis-Reference-Cited by-同舟云学术

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Deciphering the catalytic amino acid residues of l -2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1: An in silico analysis

Published:2017-10 Issue: Volume:70 Page:125-132
ISSN:1476-9271
Container-title:Computational Biology and Chemistry
language:en
Short-container-title:Computational Biology and Chemistry

Author:

Adamu Aliyu,Wahab Roswanira Abdul,Shamsir Mohd Shahir,Aliyu Firdausi,Huyop Fahrul

Funder

Malaysian Ministry of Higher Education

Bioinformatics research laboratory Universiti Teknologi Malaysia

Publisher

Elsevier BV

Subject

Computational Mathematics,Organic Chemistry,Biochemistry,Structural Biology

Reference42 articles.

1. Multi-template homology based structural model of l-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1;Adamu;J. Biomol. Struct. Dyn.,2016

2. l-2-Haloacid dehalogenase (DehL) from Rhizobium sp. RC1;Adamu;SpringerPlus,2016

3. The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold;Aravind;Trends Biochem. Sci.,1998

4. Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis;Bohác;Biochemistry,2002

5. Cloning, sequencing and expression in Escherichia coli of two Rhizobium sp. genes encoding haloalkanoate dehalogenases of opposite stereospecificity;Cairns;Eur. J. Biochem.,1996

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