BRENDA - Enzyme Database show
show all sequences of 1.3.98.3

Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli

Layer, G.; Verfurth, K.; Mahlitz, E.; Jahn, D.; J. Biol. Chem. 277, 34136-34142 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
hemeN gene, overexpression in Escherichia coli BL21(DE3)
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
C62S
inactive mutant, no Fe-S cluster formation
Escherichia coli
C66S
inactive mutant, no Fe-S cluster formation
Escherichia coli
C69S
inactive mutant, no Fe-S cluster formation
Escherichia coli
C71S
inactive mutant, same Fe-S cluster formation as in wild-type HemN
Escherichia coli
F68L
mutant with 89% of wild-type activity
Escherichia coli
G111V/G113V
double mutation of Gly-111 and Gly-113, which are part of the potential GGGTP S-adenosyl-L-methionine binding motif, completely abolishes enzyme activity, reduced Fe-S cluster formation
Escherichia coli
H58L
inactive mutant, no Fe-S cluster formation
Escherichia coli
Y56F
mutant with 45% of wild-type activity and reduced Fe-S cluster formation
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
strong inhibition
Escherichia coli
o-phenanthroline
strong inhibition
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
gel filtration in combination with glycerol gradient centrifugation
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant HemN
Escherichia coli
Reaction
Reaction
Commentary
Organism
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
catalytic, radical mechanism
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
coproporphyrinogen-III + S-adenosyl-L-methionine
HemN catalyzes the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen IX, requires S-adenosyl-L-methionine, NAD(P)H and additional cytoplasmatic components for catalysis. Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for iron-sulfur cluster formation and enzyme function. Gly-111 and Gly-113 are part of the potential GGGTP S-adenosyl-L-methionine binding motif and essential for enzymatic function, catalytic, radical mechanism
656073
Escherichia coli
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1* 52734, sequence calculation
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
requirement, oxygen-sensitive Fe-S cluster, Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for Fe-S cluster formation and enzyme function, Tyr-56 and His-58 are important for the Fe-S cluster integrity, His-58 may provide the fourth ligand besides the three cysteine residues
Escherichia coli
NADH
requires NAD(P)H, higher activity than with NADPH as cofactor
Escherichia coli
NADPH
requires NAD(P)H, lower activity than with NADH as cofactor
Escherichia coli
S-adenosyl-L-methionine
uses S-adenosyl-L-methionine as a cofactor
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
hemeN gene, overexpression in Escherichia coli BL21(DE3)
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
requirement, oxygen-sensitive Fe-S cluster, Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for Fe-S cluster formation and enzyme function, Tyr-56 and His-58 are important for the Fe-S cluster integrity, His-58 may provide the fourth ligand besides the three cysteine residues
Escherichia coli
NADH
requires NAD(P)H, higher activity than with NADPH as cofactor
Escherichia coli
NADPH
requires NAD(P)H, lower activity than with NADH as cofactor
Escherichia coli
S-adenosyl-L-methionine
uses S-adenosyl-L-methionine as a cofactor
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C62S
inactive mutant, no Fe-S cluster formation
Escherichia coli
C66S
inactive mutant, no Fe-S cluster formation
Escherichia coli
C69S
inactive mutant, no Fe-S cluster formation
Escherichia coli
C71S
inactive mutant, same Fe-S cluster formation as in wild-type HemN
Escherichia coli
F68L
mutant with 89% of wild-type activity
Escherichia coli
G111V/G113V
double mutation of Gly-111 and Gly-113, which are part of the potential GGGTP S-adenosyl-L-methionine binding motif, completely abolishes enzyme activity, reduced Fe-S cluster formation
Escherichia coli
H58L
inactive mutant, no Fe-S cluster formation
Escherichia coli
Y56F
mutant with 45% of wild-type activity and reduced Fe-S cluster formation
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
strong inhibition
Escherichia coli
o-phenanthroline
strong inhibition
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
gel filtration in combination with glycerol gradient centrifugation
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant HemN
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
coproporphyrinogen-III + S-adenosyl-L-methionine
HemN catalyzes the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen IX, requires S-adenosyl-L-methionine, NAD(P)H and additional cytoplasmatic components for catalysis. Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for iron-sulfur cluster formation and enzyme function. Gly-111 and Gly-113 are part of the potential GGGTP S-adenosyl-L-methionine binding motif and essential for enzymatic function, catalytic, radical mechanism
656073
Escherichia coli
protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1* 52734, sequence calculation
Escherichia coli
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
Other publictions for EC 1.3.98.3
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)
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739104
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Role of HemF and HemN in the h ...
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Mol. Microbiol.
96
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88
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745799
Azzouzi
Coproporphyrin III excretion ...
Rubrivivax gelatinosus
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88
339-351
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724235
Abicht
Lactococcus lactis HemW (HemN) ...
Lactococcus lactis
Biochem. J.
442
335-343
2012
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711084
Shaveta
Structural characterization re ...
Homo sapiens
Biochem. Biophys. Res. Commun.
391
1390-1395
2010
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711348
Rand
The oxygen-independent copropo ...
Escherichia coli
Biol. Chem.
391
55-63
2010
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712016
Duschene
The antiviral protein viperin ...
Homo sapiens
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584
1263-1267
2010
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713258
Goto
Functional differentiation of ...
Synechocystis sp.
Plant Cell Physiol.
51
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685280
Yokoyama
Mechanistic study on the react ...
Bacillus circulans
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47
8950-8960
2008
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686237
Frey
The radical SAM superfamily ...
Homo sapiens
Crit. Rev. Biochem. Mol. Biol.
43
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2008
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687282
Yokoyama
Characterization and mechanist ...
Bacillus circulans
J. Am. Chem. Soc.
129
15147-15155
2007
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674567
Layer
The substrate radical of Esche ...
Escherichia coli
J. Biol. Chem.
281
15727-15734
2006
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672473
Layer
Structural and functional comp ...
Bacillus subtilis, Cupriavidus necator, Escherichia coli, Rhodobacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium
Biol. Chem.
386
971-980
2005
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674462
Layer
Radical S-adenosylmethionine e ...
Escherichia coli
J. Biol. Chem.
280
29038-29046
2005
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658501
Layer
Structure and function of radi ...
Escherichia coli
Curr. Opin. Chem. Biol.
8
468-476
2004
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655340
Layer
Crystal structure of coproporp ...
Escherichia coli
EMBO J.
22
6214-6224
2003
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656073
Layer
Oxygen-independent coproporphy ...
Escherichia coli
J. Biol. Chem.
277
34136-34142
2002
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