Sandbox Reserved 1059

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This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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NrdH of Mycobacterium tuberculosis

NrdH is a redox protein part of a family of redox proteins. The other proteins that maintain the redox balance of this protein are three Thioredoxin and three glutaredoxin-like proteins. Prokaryotes typically maintain redox homeostasis through low-molecular weight thiols (glutathione) and through proteins invovled in disulfide exchange (thioredoxins).

The process of ribonucleotide reduction is one of the most fundamental biochemical process that is required for the existence of DNA-based life [1]. It is the only de novo pathway to synthesize deoxyribonucleotides. Deoxyribonucleotides are the building blocks of DNA, and they are synthesized from ribonucleotides by reducing the 2’OH in a radical based reaction. The deoxyribonucleotides are then used as precursors for the process of DNA synthesis. This reaction is catalyzed by ribonucleotide reductases (RNRs). All RNRs are related. This is evident due to the catalytic core, which is structurally conserved across all extant RNRs. RNRs are essential for the processes of DNA replication and repair (DOI: REF).

There are three classes of ribonucleotide reductases (RNRs). These classes are divided based on the mechanism of radical generation in the reaction.


Class I enzymes reduce nucleotide 5’-diphosphates, while the other 2 classes reduce ribonucleotide 5’-triphosphates [1]

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