Literature summary for 4.2.1.9 extracted from

Ren, B.; Zhang, N.; Yang, J.; Ding, H.
Nitric oxide-induced bacteriostasis and modification of iron-sulphur proteins in Escherichia coli (2008), Mol. Microbiol., 70, 953-964.

Search for more literature for 4.2.1.9

Inhibitors

Inhibitors	Comment	Organism	Structure
NO	IlvD is completely inactivated in cells by NO with the concomitant formation of the IlvD-bound dinitrosyl iron complex, DNIC. While the IlvD-bound DNIC and other protein-bound DNICs are stable in cells under anaerobic growth conditions, they are efficiently repaired under aerobic growth conditions even without new protein synthesis, L-cysteine plays an important role, overview	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	an iron-sulfur enzyme, requires an intact [4Fe-4S] cluster	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2,3-dihydroxyisovalerate	Escherichia coli	IlvD, an iron-sulfur enzyme, catalyses the conversion from 2,3-dihydroxyisovalerate to 2-keto-isovalerate and is essential for the branchend-chain amino acid biosynthesis	2-oxovalerate + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2,3-dihydroxyisovalerate	IlvD, an iron-sulfur enzyme, catalyses the conversion from 2,3-dihydroxyisovalerate to 2-keto-isovalerate and is essential for the branchend-chain amino acid biosynthesis	Escherichia coli	2-oxovalerate + H2O	-	?

Synonyms

Synonyms	Comment	Organism
dihydroxyacid dehydratase	-	Escherichia coli
IlvD	-	Escherichia coli

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Release 2023.1 (January 2023)