![]() ![]() aureus KPR functions similar to N98 of E. However, this study did not further investigate this amino acid by mutagenesis. aureus) is in the relative position as N98 for E. This study also showed that the 97 th residue in KPR ( S. coli, that KPR may exists as a dimer and functions using kinetic Cooperativity. aureus), which caused 20,000 deaths in 2017 (). However, less information mutagenic information exists for KPR found in pathogenic Staphylococcus aureus (S. When mutated, KPR was not able to function as well as the nonmutated (wildtype) KPR revealing this amino acid’s importance. One of these residues is asparagine 98 (N98), which is located in the enzyme’s active site and helps the enzyme bind the substrate. They identified key residues that are important for KPR’s function. (The interested reader is directed to Carter et al. coli) through a process called site-directed mutagenesis (SDM). (2007) investigated which amino acids are important for KPR function in Escherichia coli ( E. Studying the structure and function of KPR may accelerate the drug design process for new antibiotics. Because of this unique disparity, the pantothenate synthesis pathway has been identified as a candidate target for the development of new antibacterial drugs. However, for other organism such as prokaryotic bacteria, the synthesis of pantothenic plays a larger role in CoA production and energy metabolism. Mammals, including humans, synthesize CoA from dietary sources of pantothenic acid. CoA is an essential cofactor in energy metabolism, therefore obtaining or synthesizing pantothenic acid is important for growth and survival or an organism. KPR is one of several enzymes in the pathway that synthesizes pantothenic acid (vitamin B5), which is the substrate for coenzyme A (CoA). A pathway of central importance to energy production involves ketopantoate reductase (KPR), which catalyzes the NADPH-dependent reduction of ketopantoate to pantoate. Metabolic pathways play a critical role in energy absorption, production, and usage. Keywords: site-directed mutagenesis, ketopantoate reductase, S. Limited time in the classroom research lab prevented further work, but this research can be continued by a future student. Mutagenesis was successfully performed by mutagenic-primer based PCR as verified by restriction enzyme digestion and DNA sequencing. aureus) was mutated to GLN97 to better understand the important role that this amino acid plays. Presented here are preliminary results of an ongoing site-directed mutagenesis experiment in which ASN97 KPR ( S. Whether or not this amino acid plays an equally important role in S. ![]() coli, which have revealed ASN98 to be important for KPR function 1. ![]() A wealth of mutagenic information from previous studies is available for KPR from E. Pathogenic bacteria, not humans, rely upon KPR to power basic cellular functions and it has been identified as target for the development of new antibacterial drugs. Coenzyme A is an essential part of metabolic pathways to create energy. The enzyme Ketopantoate Reductase (KPR) catalyzes the NADPH-dependent reaction of ketopantoate to pantoate, which is ultimately converted into coenzyme A. Initial trials and tribulations towards understanding site-directed mutagenesis effects on Staphylococcus aureus ketopantoate reductase ![]()
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |