BRENDA - Enzyme Database show
show all sequences of 2.1.1.342

Radical new paradigm for heme degradation in Escherichia coli O157:H7

Lamattina, J.; Nix, D.; Lanzilotta, W.; Proc. Natl. Acad. Sci. USA 113, 12138-12143 (2016)

Data extracted from this reference:

General Stability
General Stability
Organism
the [4Fe-4S] cluster of ChuW is extremely oxygen sensitive, and enzyme activity is lost if exposed to any level of molecular oxygen
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
contain 3.8 iron atoms per monomer of purified enzyme
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin
Escherichia coli
-
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
8400
-
substrate heme, pH not specified in the publication, temperature not specified in the publication
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 S-adenosyl-L-methionine + heme + 2 reduced flavodoxin
-
741342
Escherichia coli
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
-
-
?
2 S-adenosyl-L-methionine + mesoheme + 2 reduced flavodoxin
-
741342
Escherichia coli
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
-
-
?
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin
-
741342
Escherichia coli
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
-
-
?
additional information
ChuW uses a primary carbon radical to catalyze methyl transfer and rearrangement of the porphyrin ring, resulting in the liberation of iron and opening of the porphyrin ring
741342
Escherichia coli
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
flavodoxin
-
Escherichia coli
[4Fe-4S]-center
purified protein shows a broad absorption feature with a maximum near 400 nm
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
flavodoxin
-
Escherichia coli
[4Fe-4S]-center
purified protein shows a broad absorption feature with a maximum near 400 nm
Escherichia coli
General Stability (protein specific)
General Stability
Organism
the [4Fe-4S] cluster of ChuW is extremely oxygen sensitive, and enzyme activity is lost if exposed to any level of molecular oxygen
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
contain 3.8 iron atoms per monomer of purified enzyme
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin
Escherichia coli
-
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
8400
-
substrate heme, pH not specified in the publication, temperature not specified in the publication
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 S-adenosyl-L-methionine + heme + 2 reduced flavodoxin
-
741342
Escherichia coli
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
-
-
?
2 S-adenosyl-L-methionine + mesoheme + 2 reduced flavodoxin
-
741342
Escherichia coli
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + ? + Fe2+ + 2 oxidized flavodoxin
-
-
-
?
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin
-
741342
Escherichia coli
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe2+ + 2 oxidized flavodoxin
-
-
-
?
additional information
ChuW uses a primary carbon radical to catalyze methyl transfer and rearrangement of the porphyrin ring, resulting in the liberation of iron and opening of the porphyrin ring
741342
Escherichia coli
?
-
-
-
-
Other publictions for EC 2.1.1.342
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)
740091
LaMattina
Anaerobic heme degradation: Ch ...
Escherichia coli
Biochemistry
56
845-855
2017
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741342
Lamattina
Radical new paradigm for heme ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
113
12138-12143
2016
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