BRENDA - Enzyme Database show
show all sequences of 1.14.14.B10

An alternative reaction for heme degradation catalyzed by the Escherichia coli O157H7 ChuS protein Release of hematinic acid, tripyrrole and Fe(III)

Ouellet, Y.H.; Ndiaye, C.T.; Gagne, S.M.; Sebilo, A.; Suits, M.D.; Jubinville, E.; Jia, Z.; Ivancich, A.; Couture, M.; J. Inorg. Biochem. 154, 103-113 (2016)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoporphyrin IX + ascorbate + O2
Escherichia coli
cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
hematinic acid + a tripyrrole + Fe3+
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?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
Q8X5N8
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-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
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
745504
Escherichia coli
?
-
-
-
-
protoporphyrin IX + ascorbate + O2
cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
745504
Escherichia coli
hematinic acid + a tripyrrole + Fe3+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
heme
spectrum shows bands at 409, 549, and 586 nm
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
spectrum shows bands at 409, 549, and 586 nm
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoporphyrin IX + ascorbate + O2
Escherichia coli
cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
hematinic acid + a tripyrrole + Fe3+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
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
745504
Escherichia coli
?
-
-
-
-
protoporphyrin IX + ascorbate + O2
cosubstrate is hydrogen peroxide that is formed in solution in the presence of ascorbate and O2
745504
Escherichia coli
hematinic acid + a tripyrrole + Fe3+
-
-
-
?
Other publictions for EC 1.14.14.B10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745504
Ouellet
An alternative reaction for h ...
Escherichia coli
J. Inorg. Biochem.
154
103-113
2016
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745713
Maharshak
Escherichia coli heme oxygena ...
Escherichia coli, Escherichia coli NC101
Microbiol. Immunol.
59
452-465
2015
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