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BIOCHEMISTRY Lecture Notes - Lecture 1: Pantothenic Acid, Dialysis, Paresthesia

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jaazz
21 Oct 2022
School
Kerala University of Health Sciences - KUHS
Department
Biochemistry
Course
BIOCHEMISTRY
Professor

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Document Summary

As the name suggests, it is widely distributed in nature. Pantothenic acid contains beta alanine and pantoic acid. Pantothenic acid and beta mercapto ethanol amine are parts of coenzyme a (coa). Sources of pantothenic acid: it is widely distributed in plants and animals, it is synthesised by the normal bacterial flora in intestines. Therefore, deficiency is very rare: yeast, liver and eggs are good sources. Paresthesia (burning, lightning pain) in lower extremities, Staggering gait due to impaired coordination and sleep disturbances. These deficiency manifestations are rare in human beings. The syndrome is seen during famine, in prison camps, in chronic alcoholics and in some renal dialysis patients. The beta mercapto ethanol amine (nh2 -ch2 - ch2 -sh) contains one thiol or sulfhydryl (-sh) group. It is the active site where acyl groups are carried. Therefore, the coenzyme a is sometimes abbreviated as. Acetyl-coa + choline acetyl choline + coa (enzyme is acetyl choline synthase)

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Related Questions

Rank the following B Vitamins in order of increasing molar mass.

B1, thiamine
B2, riboflavin
B5, pantothenic acid
B6, pyridoxine
B7, biotin

Pantothenic acid (vitamin B5 ) is the substrate for the biosynthesis of coenzyme A, an essential cofactor in energy metabolism. Because mammals obtain vitamin B5 from their diet, the biosynthesis of pantothenic acid in pathogenic bacteria has been identified as a drug target. Ketopantoate reductase (KPR) catalyzes the NADPH-dependent reduction of ketopantoate (KP) to pantoate, the essential precursor of pantothenic acid. Previous structural and kinetic studies have focused on Escherichia coli KPR, a monomeric enzyme with globular N- and C-terminal domains. The N terminal domain of E. coli KPR contains a Rossmann fold for binding NADPH. KP binds in the active site that is formed in the interface between the domains. The catalytic reaction follows a sequential ordered bi-bi kinetic mechanism in which the enzyme binds NADPH first, followed by KP for the hydride transfer. Here we report the structural and kinetic analysis of KPR from Staphylococcus aureus, an important human pathogen. Unlike the E. coli enzyme, S. aureus KPR forms a stable, dimeric complex that is highly conserved among several deeply divergent KPRs. Steady state analysis of the S. aureus enzyme also displays positive cooperativity with respect to the cofactor. We present evidence that the cooperativity is best explained by a random addition mechanism with a kinetically preferred path. Thus, the mechanism of S. aureus KPR is distinct from those of previously described members of the family of 2-hydroxyacid dehydrogenases.

(I always have trouble reading and comprehending scientific articles) What's the motivation for the investigation? How is the author's motivation for performing the investigation related to other work in the field?