Information on EC 1.14.14.B10 - heme oxygenase (hematinic acid-producing)

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
1.14.14.B10
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RECOMMENDED NAME
GeneOntology No.
heme oxygenase (hematinic acid-producing)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
heme + H2O2 = hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
protoheme,hydrogen peroxide oxidoreductase (porphyrin cleaving)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
protoporphyrin IX + ascorbate + O2
hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
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?
additional information
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enzyme binds and degrades heme in a reaction that releases carbon monoxide. Initial intermediates of the reaction of ChuS with hydrogen peroxide, i.e. a ferrous keto pi neutral radical and ferric verdoheme, are in common with heme oxygenases, while a further reaction step, involving the cleavage of the porphyrin ring at adjacent meso-carbons, results in the release of hematinic acid, a tripyrrole product and non-heme iron in the ferric oxidation state
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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
protoporphyrin IX + ascorbate + O2
hematinic acid + a tripyrrole + Fe3+
show the reaction diagram
Q8X5N8
cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
spectrum shows bands at 409, 549, and 586 nm
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
incubation of strain NC101 with an iron chelator results in more than 300fold increase in ChuS mRNA expression