HALOACID DEHALOGENASE FROM KLEBSIELLA PNEUMONIAE ITB1 IN PET-HAKP1 RECOMBINANT CLONE

• Main Author: Desy Venorita, Siahaan
• Format: Final Project
• Language: Indonesia
• Subjects: Kimia
• Online Access: https://digilib.itb.ac.id/gdl/view/49119
• Institution: Institut Teknologi Bandung

Organohalogens are organic compounds that has a covalent bond between the carbon and halogen atom in their structure. Organohalogen compounds are widely used as raw materials in the manufacture process of other materials, including herbicides, plastics, and PVCs. However, organohalogen compounds are also pollutants for the environment due to their persistent and toxic nature. One method that can be done to decrease organohalogen pollution is by bioremediation using microorganisms that are capable of producing haloacid dehalogenase, an enzyme that can degrade organohalogens. It is known that haloacid dehalogenase is classified into Group I (DehI) and Group II (DehII). The dehalogenation process by DehI involves the nucleophile attack by a water molecule to C2 carbon on the substrate without the formation of enzyme-substrate intermediates. Whereas the dehalogenation process by DehII involves the attack of aspartic acid recidues as nucleophile to the C2 carbon on the substrate, forming an esterified enzyme-substrate intermediate. Previous studies have successfully cloned and sequenced the haloacid dehalogenase gene from Klebsiella pneumoniae ITB1. The purpose of this research is to study and classify the haloacid dehalogenae (Hakp1) protein from Klebsiella pneumoniae ITB1. The 3D structure prediction using SWISS-MODEL shows that the Hakp1 structure consists of a cap domain and core domain with ?/? type. The results of the superimposed 3D structure of Hakp1 showed a similarity to the E1 enolase fosfatase protein from Homo sapiens and the L- haloacid dehalogenase protein from Pseudomonas sp. YL with RMSD values of respectively 0,108 Å and 0,168 Å. This superimposed result also shows that Hakp1 is DehII with an Asp8 residues act as nucleophile.