Structure Prediction of Delta Aminolevulinic Acid Dehydratase (ALAD); An Enzyme that is Very Sensitive to the Toxic Effects of LeadZahra Batool* and Asma Haque
Department of Bioinformatics and Biotechnology, Quaid-i-Azam University Islamabad, Pakistan
- *Corresponding Author:
- Zahra Batool
Department of Bioinformatics and Biotechnology
Quaid-i-Azam University Islamabad, 45320, Pakistan
Tel: +92- 051 9064 0000
E-mail: [email protected]
Received date: September 28, 2015; Accepted date: October 17, 2015; Published October 26, 2015
Citation: Batool Z, Haque A (2015) Structure Prediction of Delta Aminolevulinic Acid Dehydratase (ALAD); An Enzyme that is Very Sensitive to the Toxic Effects of Lead. J Biom Biostat 6: 259. doi:10.4172/2155-6180.1000259
Copyright:© 2015 Batool Z, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
The ALAD (Aminolevulinic Acid Dehydratase) gene polymorphism is linked with the accumulation of lead in the bone, blood and the other internal organs and it may predispose for many critical symptoms in the lead exposed persons. The aim of this study is to determine the primary, secondary and tertiary structure of lead. This enzyme is susceptible towards the toxic effect of lead. Primary structure prediction was done by Protparam tool, Compute PI/MW tool, Proscale tool. Secondary structure prediction was done by Self –optimize prediction method (SOPMA) tool, Porter tool. Tertiary structure prediction was done by protein structure prediction server. Domain was determined by Simple Modular Architecture Research (SMART) tool.