Alinne Batista Ambrosio
Brazil
Research Article
In-silico Identification of Candidate Inhibitory Ligands against Ornithine Decarboxylase Enzyme for Human Sleeping Sickness Causing Trypanosoma brucei
Author(s): Hukkeri S and Alinne Batista Ambrosio
Hukkeri S and Alinne Batista Ambrosio
Ornithine Decarboxylase (ODC) catalyzes the decarboxylation of ornithine to putrescine. This is known to be a crucial step in the biosynthesis of polyamines. These polyamines are necessary for microbial cell growth and proliferation. Hence, ODC enzyme is the best target to treat African sleeping sickness disease-causing protozoan parasite, Trypanosoma brucei. ODC is a 5'-pyridoxal phosphate (PLP) dependent, an obligate homodimer enzyme with two identical active sites at the dimer interface, comprising the beta or alpha barrel domain from one subunit and beta-sheet domain from the other subunit. The catalytic residues are contributed to the active site from both monomers. An X-ray crystallography study on ODC in the wild T. brucei has revealed two structural changes upon ligand binding; an amino acid residue specifically Lys-69 is displaced by putrescine forming a new interaction and a si.. View More»
DOI:
10.4172/2167-7956.1000148