EC Explorer

3.1.1.109

iron(III)-salmochelin esterase

(1) iron(III)-[diglucosyl-enterobactin] complex + H₂O = iron(III)-[salmochelin S2] complex;;(2) iron(III)-[monoglucosyl-enterobactin] complex + H₂O = iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)₃] complex;;(3) iron(III)-[salmochelin S2] complex + H₂O = iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)₂] complex + N-(2,3-dihydroxybenzoyl)-L-serine;;(4) iron(III)-[salmochelin S2] complex + H₂O = iron(III)-[salmochelin S1] complex + salmochelin SX;;(5) iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)₃] complex + H₂O = iron(III)-[salmochelin S1] complex + N-(2,3-dihydroxybenzoyl)-L-serine;;(6) iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)₂] complex + H₂O = iron(III)-[salmochelin SX] complex + salmochelin SX

iroD (gene name), ferric-salmochelin esterase

iron(III)-salmochelin complex hydrolase

This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. The enzyme acts on iron(III)-bound enterobactin and C-glucosylated derivatives known as salmochelins. Unlike EC 3.1.1.107, apo-salmochelin esterase (IroE), IroD prefers iron(III)-bound siderophores as substrates, and is assumed to act after the iron-siderophore complexes are imported into the cell. It catalyses several hydrolytic reactions, producing a mixture of iron(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] complex and salmochelin SX.

created 2019