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Literature summary extracted from

  • Palmer, D.J.; Schroeder, S.; Lawrence, A.D.; Deery, E.; Lobo, S.A.; Saraiva, L.M.; McLean, K.J.; Munro, A.W.; Ferguson, S.J.; Pickersgill, R.W.; Brown, D.G.; Warren, M.J.
    The structure, function and properties of sirohaem decarboxylase - an enzyme with structural homology to a transcription factor family that is part of the alternative haem biosynthesis pathway (2014), Mol. Microbiol., 93, 247-261.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.111 expression in Escherichioa coli Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Methanosarcina barkeri DSM 804 the enzyme is involved in the alternative heme biosynthesis pathway (in bacteria and archaea) 12,18-didecarboxysiroheme + 2 CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.111 Methanosarcina barkeri Q46CH6 and Q46CH5 Q46CH6: subunit AhbA, Q46CH5: subunit AhbB
-
4.1.1.111 Methanosarcina barkeri DSM 804 Q46CH6 and Q46CH5 Q46CH6: subunit AhbA, Q46CH5: subunit AhbB
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 siroheme yield 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 was due to loss of the carboxylic acid from the C12 or C18 side-chain. AhbA and AhbB together catalyze the conversion of siroheme into 12,18-didecarboxysiroheme Methanosarcina barkeri 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 DSM 804 12,18-didecarboxysiroheme + 2 CO2
-
 ?
4.1.1.111 siroheme incubations of individual AhbA and AhbB proteins in excess with siroheme yield 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 was due to loss of the carboxylic acid from the C12 or C18 side-chain. AhbA and AhbB together catalyze the conversion of siroheme into 12,18-didecarboxysiroheme Methanosarcina barkeri DSM 804 12,18-didecarboxysiroheme + 2 CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.111 heterodimer subunit AhbA and subunit AhbB form a heterodimeric heme-binding complex Methanosarcina barkeri

Synonyms

EC Number Synonyms Comment Organism
4.1.1.111 AhbAB
-
 Methanosarcina barkeri
4.1.1.111 Mbar A1459/Mbar A1460 locus names Methanosarcina barkeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.111 37
-
 assay at Methanosarcina barkeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.111 7.5
-
 assay at Methanosarcina barkeri

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.111 heme subunit AhbA and subunit AhbB form a heterodimeric heme-binding complex Methanosarcina barkeri

General Information

EC Number General Information Comment Organism
4.1.1.111 physiological function the enzyme is involved in the alternative haem biosynthesis pathway (in bacteria and archaea) Methanosarcina barkeri