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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.9 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

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.9 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

EC Number Organism UniProt Comment Textmining
4.2.1.9 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.9 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

EC Number Synonyms Comment Organism
4.2.1.9 dihydroxyacid dehydratase
-
 Escherichia coli
4.2.1.9 IlvD
-
 Escherichia coli