Journal of Biotechnology & Biomaterials
Open Access

Abstract

The development of anti-parasitic agent is quite challenging particularly when exploiting biochemical differences between the parasite and the host. However, with post-genome bioinformatics and experimental research, drug targets can be more easily identified. Ribose metabolism in protozoans is of interest because protozoa in general are auxotrophic for purines and acquire these nutrients from the hosts. Ribose is utilized in the production of ribose 5-phosphate required for the synthesis of 5-phosphoribosyl- 1-pyrophosphate that is used with purine bases for the synthesis of nucleic acids. The enzyme responsible for the conversion of ribose to ribose 5-phosphate is ribokinase. The gene for ribokinase of Leishmania was cloned and expressed in E. coli. It has 990 base pairs and encodes a 329 amino acid protein. Biochemical characteristic of the enzyme shows that ribokinase is highly specific for D-ribose although it insignificantly phosphorylates other five- and six-carbon sugars like D-arabinose, D-xylose, D-galactose and D-fructose. The catalytic efficiency for D-ribose catalysis ranges from 10.8 s-1 mM-1 to 40.6 s-1 mM-1. The enzyme has absolute requirement for inorganic phosphate.

Biography

Patrick O Ogbunude obtained a Master’s degree from University of Alberta, Canada and PhD from Ahmadu Bello University in Nigeria and thereafter did research in several laboratories in various places including defunct International Laboratory for Research in Animal Diseases, Nairobi Kenya, King Faisal Special Hospital and Research Centre, Riyadh Kingdom of Saudi Arabia and The University of Glasgow, Scotland, UK. He has made several seminal discoveries like the identification of purine nucleoside hydrolase activity in trypanosomes and channel like properties of nucleoside transporters in Leishmania. He has considerable experience in research with over fifty-six research papers in peer reviewed journals.

Email: ogbunudejim@yahoo.co.uk