EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
4.99.1.4 | precorrin-2 + Co2+ |
SirB, much lower specific activity than with sirohydrochlorin |
Priestia megaterium |
cobalt-precorrin-2 + 2 H+ |
- |
? |
4.99.1.4 | precorrin-2 + Co2+ |
SirB, much lower specific activity than with sirohydrochlorin |
Priestia megaterium DSM 509 |
cobalt-precorrin-2 + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Co2+ |
- |
Salmonella enterica |
cobalt-sirohydrochlorin + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Co2+ |
- |
Saccharomyces cerevisiae |
cobalt-sirohydrochlorin + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Co2+ |
SirB, lower specificity for cobalt than for iron |
Priestia megaterium |
cobalt-sirohydrochlorin + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Co2+ |
SirB, lower specificity for cobalt than for iron |
Priestia megaterium DSM 509 |
cobalt-sirohydrochlorin + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Co2+ |
pH 8.0 |
Arabidopsis thaliana |
cobalt-sirohydrochlorin + H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Fe2+ |
CysG structure, the multifunctional siroheme synthase CysG synthesizes siroheme from uroporphyrinogen III, CysG contains two structurally independent modules: a bismethyltransferase and a dual-function dehydrogenase-chelatase |
Salmonella enterica |
siroheme + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Fe2+ |
Met8p catalyzes ferrochelation during the synthesis of siroheme, both ferrochelation and NAD+-dependent dehydrogenation of preccorin-2 to produce sirohydrochlorin take place in a single bifunctional active site, Asp-141 participates in both catalytic reactions, which are not linked mechanistically, mechanism |
Saccharomyces cerevisiae |
siroheme + 2 H+ |
- |
? |
4.99.1.4 | sirohydrochlorin + Fe2+ |
Met8p structure, bifunctional Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme, both catalytic activities share a single active site, Asp-141 functions as a general base and plays an essential role in both dehydrogenase and chelatase processes |
Saccharomyces cerevisiae |
siroheme + 2 H+ |
- |
? |