EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.141 | Dithionite | presence of reducing agents is essential, and dithionite is most effective among reagents tested | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.5.1.141 | cytoplasmic membrane | - |
Escherichia coli | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.141 | Ca2+ | the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protohemMe and farnesyl diphosphate to heme i n the presence of divalent cations such as Mg2+ or Ca2+ | Escherichia coli | |
2.5.1.141 | Mg2+ | the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protohemMe and farnesyl diphosphate to heme i n the presence of divalent cations such as Mg2+ or Ca2+ | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.141 | 26000 | - |
x * 26000, SDS-PAGE | Escherichia coli |
2.5.1.141 | 28000 | - |
x * 28000, urea-SDS-PAGE | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.141 | protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | Escherichia coli | - |
heme o + diphosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.141 | Escherichia coli | P0AEA5 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.141 | protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | - |
Escherichia coli | heme o + diphosphate | - |
? | |
2.5.1.141 | protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme and farnesyl diphosphate to heme in the presence of divalent cations such as Mg2+ or Ca2+. The CyoE protein in vitro catalyzes a direct transfer of the farnesyl moiety from a farnesyl diphosphate-Mg2+ complex to position 2 of the vinyl group at pyrrole ring D of ferrous protoheme M, possibly by a one-step reaction | Escherichia coli | heme o + diphosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.141 | ? | x * 26000, SDS-PAGE | Escherichia coli |
2.5.1.141 | ? | x * 28000, urea-SDS-PAGE | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.141 | cyoE | - |
Escherichia coli |
2.5.1.141 | heme B farnesyltransferase | - |
Escherichia coli |
2.5.1.141 | heme o synthase | - |
Escherichia coli |
2.5.1.141 | JW0418 | locus name | Escherichia coli |