EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.111 | Dithionite | the haem bound to the AhbA/B complex must be reduced in order for the enzyme to be most active. Treatment with excess dithionite results in a 6.5fold increase in the activity of the enzyme | Desulfovibrio desulfuricans | |
4.1.1.111 | Dithionite | the heme bound to the AhbA/B complex must be reduced in order for the enzyme to be most active. Treatment with excess dithionite results in a 6.5fold increase in the activity of the enzyme | Methanosarcina barkeri |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.111 | proteins ahbA and ahbB are cloned into distinct plasmids and expressed separately in Escherichia coli. When expressed individually the encoded proteins are highly unstable and can only be purified at very low concentrations due to their tendency to precipitate | Desulfovibrio desulfuricans |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.1.111 | hanging drop vapour diffusion crystallization at 19°C | Desulfovibrio desulfuricans |
EC Number | General Stability | Organism |
---|---|---|
4.1.1.111 | subunits AhbA and AhbB have a stabilizing effect on each other by forming a complex | Desulfovibrio desulfuricans |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.111 | monodecarboxysiroheme | single active site with a competitive inhibition model for siroheme and monodecarboxysiroheme | Desulfovibrio desulfuricans | |
4.1.1.111 | siroheme | single active site with a competitive inhibition model for siroheme and monodecarboxysiroheme | Desulfovibrio desulfuricans |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.111 | 44000 | - |
heterodimeric complex of subunits AhbA and AhbB, gel filtration | Desulfovibrio desulfuricans |
4.1.1.111 | 94000 | - |
heterotetrameric complex of subunits AhbA and AhbB, gel filtration | Desulfovibrio desulfuricans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.111 | siroheme | Desulfovibrio desulfuricans | - |
12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | Methanosarcina barkeri | the enzyme is involved in the alternative heme biosynthesis pathway (in bacteria and archaea) | 12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | Desulfovibrio desulfuricans DSM 6949 | - |
12,18-didecarboxysiroheme + 2 CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.111 | Desulfovibrio desulfuricans | B8J364 | - |
- |
4.1.1.111 | Desulfovibrio desulfuricans DSM 6949 | B8J364 | - |
- |
4.1.1.111 | Methanosarcina barkeri | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.111 | proteins ahbA and ahbB are cloned into distinct plasmids and expressed separately in Escherichia coli. When expressed individually the encoded proteins are highly unstable and can only be purified at very low concentrations due to their tendency to precipitate | Desulfovibrio desulfuricans |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.111 | siroheme | - |
Methanosarcina barkeri | 12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | - |
Desulfovibrio desulfuricans | 12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | the enzyme is involved in the alternative heme biosynthesis pathway (in bacteria and archaea) | Methanosarcina barkeri | 12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | incubations of individual AhbA and AhbB proteins in excess with sirohaem yields mixtures with varying levels of siroheme, monodecarboxysiroheme and didecarboxysiroheme. The monodecarboxysiroheme is not characterized further and hence it is not determined as to whether it is due to loss of the carboxylic acid from the C12 or C18 side-chain. The individual subunits, AhbA and AhbB, are capable of decarboxylating siroheme by themselves. The individual subunits form homodimers, which likely represents the active species | Desulfovibrio desulfuricans | 12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | - |
Desulfovibrio desulfuricans DSM 6949 | 12,18-didecarboxysiroheme + 2 CO2 | - |
? | |
4.1.1.111 | siroheme | incubations of individual AhbA and AhbB proteins in excess with sirohaem yields mixtures with varying levels of siroheme, monodecarboxysiroheme and didecarboxysiroheme. The monodecarboxysiroheme is not characterized further and hence it is not determined as to whether it is due to loss of the carboxylic acid from the C12 or C18 side-chain. The individual subunits, AhbA and AhbB, are capable of decarboxylating siroheme by themselves. The individual subunits form homodimers, which likely represents the active species | Desulfovibrio desulfuricans DSM 6949 | 12,18-didecarboxysiroheme + 2 CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.111 | heterodimer | composed of AhbA and AhbB | Methanosarcina barkeri |
4.1.1.111 | heterodimer | the individual subunits, AhbA and AhbB, are capable of decarboxylating sirohaem by themselves. The individual subunits form homodimers, which likely represents the active species. Subunits AhbA and AhbB have a stabilizing effect on each other by forming a complex | Desulfovibrio desulfuricans |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.111 | AhbA/B | - |
Methanosarcina barkeri |
4.1.1.111 | sirohaem decarboxylase | - |
Methanosarcina barkeri |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.111 | heme | the heme bound to the AhbA/B complex must be reduced in order for the enzyme to be most active. Treatment with excess dithionite results in a 6.5fold increase in the activity of the enzyme | Methanosarcina barkeri |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.1.111 | physiological function | the enzyme is involved in the alternative heme biosynthesis pathway (in bacteria and archaea) | Desulfovibrio desulfuricans |
4.1.1.111 | physiological function | the enzyme is involved in the alternative heme biosynthesis pathway (in bacterioa and archaea) | Methanosarcina barkeri |