Information on EC 4.1.1.B11 - siroheme decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.1.1.B11
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
siroheme decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
siroheme = 12,18-didecarboxysiroheme + 2 CO2
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
heme metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
siroheme carboxy-lyase (12,18-didecarboxysiroheme-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q46CH6: subunit AhbA, Q46CH5: subunit AhbB
Q46CH6 and Q46CH5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
siroheme
12,18-didecarboxysiroheme + 2 CO2
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
siroheme
12,18-didecarboxysiroheme + 2 CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
monodecarboxysiroheme
single active site with a competitive inhibition model for siroheme and monodecarboxysiroheme
siroheme
single active site with a competitive inhibition model for siroheme and monodecarboxysiroheme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithionite
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
Q46CH6 and Q46CH5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Q46CH6 and Q46CH5
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
heterodimeric complex of subunits AhbA and AhbB, gel filtration
94000
heterotetrameric complex of subunits AhbA and AhbB, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion crystallization at 19°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
subunits AhbA and AhbB have a stabilizing effect on each other by forming a complex
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichioa coli
Q46CH6 and Q46CH5
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