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SUMMARY:A Systematic Integration of Empirical and Computational Studies to
  Biophysically Describe Recombinant Nicotinate Mononucleotide Adenylyltran
 sferase (NaMNAT) From Klebsiella pneumonia
DTSTART;VALUE=DATE-TIME:20210322T140000Z
DTEND;VALUE=DATE-TIME:20210322T142000Z
DTSTAMP;VALUE=DATE-TIME:20260711T205836Z
UID:indico-contribution-6938@events.saip.org.za
DESCRIPTION:Speakers: Olamide Jeje ()\nNicotinate mononucleotide adenylylt
 ransferase (NaMNAT) is an indispensable enzyme in the biosynthesis of pyri
 dine dinucleotides. Given the vital role of NAD+ in controlling key cellul
 ar processes\, NaMNAT represents an attractive target for the design of no
 vel broad-spectrum antibiotics to treat nosocomial infections associated w
 ith MDR Klebsiella Pneumonia. This study aims to characterize the biophysi
 cal structure of NaMNAT from K. Pneumonia (KpNaMNAT) using a systematic co
 mbination of experimental and computational approaches. Overexpression and
  purification were carried out using hexa-histidine tags in E. coli expres
 sion system and nickel ion-immobilized metal affinity chromatography. Acti
 vity studies using NMN substrate showed KpNaMNAT to demonstrate broad pH o
 ptima of 6.5-9.5 and preference for Mg2+. Structural characterisation reve
 aled KpNaMNAT as a monomer with predominate α-helices. ATP\, NMN\, and NA
 D+ all bind at the same site on KpNaMNAT\, but do not induce any significa
 nt conformational changes\, however\, ATP responds to Mg2+ more than the o
 ther ligands and the protein response in the presence of Mg2+. The data an
 d insight provided by this novel research would be useful as a molecular b
 asis for further evaluation of the enzymes for the design of structure-bas
 ed inhibitors with therapeutic potential.\n\nhttps://events.saip.org.za/ev
 ent/213/contributions/6938/
LOCATION:Zoom Conference
URL:https://events.saip.org.za/event/213/contributions/6938/
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