BRENDA - Enzyme Database show
show all sequences of 2.5.1.141

In vitro heme O synthesis by the cyoE gene product from Escherichia coli

Saiki, K.; Mogi, T.; Ogura, K.; Anraku, Y.; J. Biol. Chem. 268, 26041-26044 (1993)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Dithionite
presence of reducing agents is essential, and dithionite is most effective among reagents tested
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasmic membrane
-
Escherichia coli
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protohemMe and farnesyl diphosphate to heme i n the presence of divalent cations such as Mg2+ or Ca2+
Escherichia coli
Mg2+
the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protohemMe and farnesyl diphosphate to heme i n the presence of divalent cations such as Mg2+ or Ca2+
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
x * 26000, SDS-PAGE
Escherichia coli
28000
-
x * 28000, urea-SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
Escherichia coli
-
heme o + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AEA5
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
-
727810
Escherichia coli
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme and farnesyl diphosphate to heme in the presence of divalent cations such as Mg2+ or Ca2+. The CyoE protein in vitro catalyzes a direct transfer of the farnesyl moiety from a farnesyl diphosphate-Mg2+ complex to position 2 of the vinyl group at pyrrole ring D of ferrous protoheme M, possibly by a one-step reaction
727810
Escherichia coli
heme o + diphosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 26000, SDS-PAGE; x * 28000, urea-SDS-PAGE
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Dithionite
presence of reducing agents is essential, and dithionite is most effective among reagents tested
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasmic membrane
-
Escherichia coli
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protohemMe and farnesyl diphosphate to heme i n the presence of divalent cations such as Mg2+ or Ca2+
Escherichia coli
Mg2+
the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protohemMe and farnesyl diphosphate to heme i n the presence of divalent cations such as Mg2+ or Ca2+
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
x * 26000, SDS-PAGE
Escherichia coli
28000
-
x * 28000, urea-SDS-PAGE
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
Escherichia coli
-
heme o + diphosphate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
-
727810
Escherichia coli
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme and farnesyl diphosphate to heme in the presence of divalent cations such as Mg2+ or Ca2+. The CyoE protein in vitro catalyzes a direct transfer of the farnesyl moiety from a farnesyl diphosphate-Mg2+ complex to position 2 of the vinyl group at pyrrole ring D of ferrous protoheme M, possibly by a one-step reaction
727810
Escherichia coli
heme o + diphosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 26000, SDS-PAGE; x * 28000, urea-SDS-PAGE
Escherichia coli
Other publictions for EC 2.5.1.141
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)
743825
Stevens
Cytolytic toxin production by ...
Staphylococcus aureus, Staphylococcus aureus JE2
Sci. Rep.
7
13744
2017
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2
2
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727913
Khalimonchuk
Oligomerization of heme o synt ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
J. Biol. Chem.
287
26715-26726
2012
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6
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6
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1
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1
1
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727792
Mogi T.
Over-expression and characteri ...
Bacillus subtilis
J. Biochem.
145
669-675
2009
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1
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1
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3
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1
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727866
Wang
Regulation of the heme A biosy ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
J. Biol. Chem.
284
839-847
2009
1
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1
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5
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1
1
1
1
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726940
Brown
Heme O synthase and heme A syn ...
Bacillus subtilis, Bacillus subtilis 168, Rhodobacter sphaeroides, Rhodobacter sphaeroides DSM 158
Biochemistry
43
13541-13548
2004
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2
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9
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2
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2
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727609
Valnot
A mutation in the human heme A ...
Homo sapiens
Hum. Mol. Genet.
9
1245-1249
2000
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1
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1
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3
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1
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727597
Murakami
Genomic structure and expressi ...
Homo sapiens
Genomics
42
161-164
1997
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2
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16
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16
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741946
Malakhov
The coxD gene for heme O synt ...
Synechocystis sp. PCC 6803
Biochim. Biophys. Acta
1273
84-86
1996
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4
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728704
Glerum
Isolation of a human cDNA for ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
91
8452-8456
1994
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1
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742503
Saiki
An Escherichia coli cyoE gene ...
Bacillus sp. PS3
FEBS Lett.
351
385-388
1994
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1
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1
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3
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1
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726848
Saiki
Heme O biosynthesis in Escheri ...
Escherichia coli
Biochem. Biophys. Res. Commun.
189
1491-1497
1993
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727810
Saiki
In vitro heme O synthesis by t ...
Escherichia coli
J. Biol. Chem.
268
26041-26044
1993
1
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2
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727811
Saiki
Identification of the function ...
Escherichia coli
J. Biol. Chem.
268
26927-16934
1993
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40
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3
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40
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743298
Svensson
Bacillus subtilis CtaA and Ct ...
Bacillus subtilis
Mol. Microbiol.
10
193-201
1993
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1
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5
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