BRENDA - Enzyme Database show
show all sequences of 2.5.1.141

Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2

Khalimonchuk, O.; Kim, H.; Watts, T.; Perez-Martinez, X.; Winge, D.R.; J. Biol. Chem. 287, 26715-26726 (2012)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
188K/P217L
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The double T188K/P217L mutant is unable to support respiratory growth, and cytochrome c oxidase activity in the mutant cells is markedly attenuated. Unstable mutant enzyme
Saccharomyces cerevisiae
E328G
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The E328G Cox10 mutant supports respiratory growth and contributes to appreciable cytochrome c oxidase activity
Saccharomyces cerevisiae
E328V
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. Cells containing the E328V Cox10 are impaired in respiration and cytochrome c oxidase activity
Saccharomyces cerevisiae
P217L
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The P217L Cox10 variant supports glycerol/lactate growth, but cytochrome c oxidase activity is slightly impaired
Saccharomyces cerevisiae
T188K
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. Cells harboring T188K Cox10 are partially compromised in respiratory growth. Mutant enzyme is unstable
Saccharomyces cerevisiae
T188K/N196K
the double mutant exhibits no enhanced protein stability, and the cells are more compromised in glycerol/lactate growth and cytochrome c oxidase activity, compared with the single T188K mutant
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
heme o + diphosphate
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
Saccharomyces cerevisiae ATCC 204508
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
heme o + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P21592
-
-
Saccharomyces cerevisiae ATCC 204508
P21592
-
-
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
-
727913
Saccharomyces cerevisiae
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
727913
Saccharomyces cerevisiae
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
-
727913
Saccharomyces cerevisiae ATCC 204508
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
727913
Saccharomyces cerevisiae ATCC 204508
heme o + diphosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
oligomer
the active state of Cox10 appears to be a homo-oligomeric complex, and formation of this complex is dependent on the newly synthesized CcO subunit Cox1 and the presence of an early Cox1 assembly intermediate. Cox10 multimerization is triggered by progression of Cox1 from the early assembly intermediate to downstream intermediates. The CcO assembly factor Coa2 appears important in coupling the presence of newly synthesized Cox1 to Cox10 oligomerization
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
188K/P217L
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The double T188K/P217L mutant is unable to support respiratory growth, and cytochrome c oxidase activity in the mutant cells is markedly attenuated. Unstable mutant enzyme
Saccharomyces cerevisiae
E328G
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The E328G Cox10 mutant supports respiratory growth and contributes to appreciable cytochrome c oxidase activity
Saccharomyces cerevisiae
E328V
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. Cells containing the E328V Cox10 are impaired in respiration and cytochrome c oxidase activity
Saccharomyces cerevisiae
P217L
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The P217L Cox10 variant supports glycerol/lactate growth, but cytochrome c oxidase activity is slightly impaired
Saccharomyces cerevisiae
T188K
mutation is introduced into yeast COX10 and tested in cox10DELTA cells. Cells harboring T188K Cox10 are partially compromised in respiratory growth. Mutant enzyme is unstable
Saccharomyces cerevisiae
T188K/N196K
the double mutant exhibits no enhanced protein stability, and the cells are more compromised in glycerol/lactate growth and cytochrome c oxidase activity, compared with the single T188K mutant
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
heme o + diphosphate
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
Saccharomyces cerevisiae ATCC 204508
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
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
-
727913
Saccharomyces cerevisiae
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
727913
Saccharomyces cerevisiae
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
-
727913
Saccharomyces cerevisiae ATCC 204508
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
727913
Saccharomyces cerevisiae ATCC 204508
heme o + diphosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
oligomer
the active state of Cox10 appears to be a homo-oligomeric complex, and formation of this complex is dependent on the newly synthesized CcO subunit Cox1 and the presence of an early Cox1 assembly intermediate. Cox10 multimerization is triggered by progression of Cox1 from the early assembly intermediate to downstream intermediates. The CcO assembly factor Coa2 appears important in coupling the presence of newly synthesized Cox1 to Cox10 oligomerization
Saccharomyces cerevisiae
General Information
General Information
Commentary
Organism
metabolism
the synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase
Saccharomyces cerevisiae
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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5
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1
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6
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4
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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1
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5
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1
1
1
1
-
-
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
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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1
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4
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1
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1
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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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3
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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
1
1
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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727811
Saiki
Identification of the function ...
Escherichia coli
J. Biol. Chem.
268
26927-16934
1993
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40
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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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