Literature summary extracted from

Van Laer, K.; Buts, L.; Foloppe, N.; Vertommen, D.; Van Belle, K.; Wahni, K.; Roos, G.; Nilsson, L.; Mateos, L.M.; Rawat, M.; van Nuland, N.A.; Messens, J.
Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of mycobacteria (2012), Mol. Microbiol., 86, 787-804.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.20.4.3	solution structures of oxidized and reduced mycoredoxin-1 reveal a thioredoxin fold with a putative mycothiol-binding site	Mycolicibacterium smegmatis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.20.4.3	Mycolicibacterium smegmatis	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.20.4.3	additional information	isoform mycoredoxin-1 gets S-mycothiolated on its N-terminal nucleophilic cysteine residue	Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.20.4.3	additional information	isoform mycoredoxin-1 acts as an oxidoreductase exclusively linked to the mycothiol electron transfer pathway and can reduce S-mycothiolated mixed disulfides. Mycoredoxin-1 has a redox potential of -218 mV and hydrogen bonding with neighbouring residues lowers the pKa of its N-terminal nucleophilic cysteine	Mycolicibacterium smegmatis	?	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.20.4.3	mycoredoxin-1	-	Mycolicibacterium smegmatis

General Information

EC Number	General Information	Comment	Organism
1.20.4.3	physiological function	a mycoredoxin-1 deletion strain is more sensitive to oxidative stress than wild-type	Mycolicibacterium smegmatis

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Release 2023.1 (January 2023)