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(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
overexpression of the cyoE gene in a cyo operon deletion strain results in a conversion of protoheme IX to heme 0
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
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
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
the enzyme catalyzes the first step in the conversion of protoheme to the heme A prosthetic groups of the cytochrome c oxidase
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
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
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
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
-
-
?
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(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + protoheme IX + H2O
diphosphate + ferroheme o
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
-
-
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
the enzyme catalyzes the first step in the conversion of protoheme to the heme A prosthetic groups of the cytochrome c oxidase
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
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
-
-
?
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
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
-
-
?
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Acidosis
Sideroblastic anemia associated with multisystem mitochondrial disorders.
Acidosis, Renal Tubular
Sideroblastic anemia associated with multisystem mitochondrial disorders.
Anemia
Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency.
Anemia
Sideroblastic anemia associated with multisystem mitochondrial disorders.
Anemia, Sideroblastic
Comment on: Sideroblastic anemia associated with multisystem mitochondrial disorders: The phenotypic spectrum of PUS1 and COX10 variants and mtDNA deletions needs to be prospectively assessed.
Azoospermia
[Expression of COX10 in human non-obstructive azoospermia testes]
Cardiomyopathies
Cardiomyopathy in children with mitochondrial disease: Prognosis and genetic background.
Cardiomyopathy, Hypertrophic
Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency.
Cardiomyopathy, Hypertrophic
Sideroblastic anemia associated with multisystem mitochondrial disorders.
Coma
Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy.
Coronary Artery Disease
RNA-sequencing reveals that STRN, ZNF484 and WNK1 add to the value of mitochondrial MT-COI and COX10 as markers of unstable coronary artery disease.
Cytochrome-c Oxidase Deficiency
A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency.
Cytochrome-c Oxidase Deficiency
Bezafibrate improves mitochondrial function in the CNS of a mouse model of mitochondrial encephalopathy.
Cytochrome-c Oxidase Deficiency
COX10 Mutations Resulting in Complex Multisystem Mitochondrial Disease That Remains Stable Into Adulthood.
Cytochrome-c Oxidase Deficiency
Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals.
Cytochrome-c Oxidase Deficiency
Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency.
Cytochrome-c Oxidase Deficiency
Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency.
Cytochrome-c Oxidase Deficiency
Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy.
Cytochrome-c Oxidase Deficiency
[A case with cytochrome C oxidase deficiency caused by COX10 gene variation].
Deafness
Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency.
Death, Sudden, Cardiac
A Novel COX10 Deletion Polymorphism as a Susceptibility Factor for Sudden Cardiac Death Risk in Chinese Populations.
Glomerulosclerosis, Focal Segmental
Deletion of the mitochondrial complex-IV co-factor heme A:farnesyltransferase causes focal segmental glomerulosclerosis and interferon response.
heme o synthase deficiency
COX10 Mutations Resulting in Complex Multisystem Mitochondrial Disease That Remains Stable Into Adulthood.
Infections
Reliance on Cox10 and oxidative metabolism for antigen-specific NK cell expansion.
Leigh Disease
Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency.
Leigh Disease
Oligomerization of Heme o Synthase in Cytochrome Oxidase Biogenesis Is Mediated by Cytochrome Oxidase Assembly Factor Coa2.
Microcephaly
Sideroblastic anemia associated with multisystem mitochondrial disorders.
Mitochondrial Diseases
Comment on: Sideroblastic anemia associated with multisystem mitochondrial disorders: The phenotypic spectrum of PUS1 and COX10 variants and mtDNA deletions needs to be prospectively assessed.
Mitochondrial Diseases
COX10 Mutations Resulting in Complex Multisystem Mitochondrial Disease That Remains Stable Into Adulthood.
Mitochondrial Diseases
Cytochrome c Oxidase Activity Is a Metabolic Checkpoint that Regulates Cell Fate Decisions During T Cell Activation and Differentiation.
Mitochondrial Diseases
Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency.
Mitochondrial Diseases
Sideroblastic anemia associated with multisystem mitochondrial disorders.
Mitochondrial Myopathies
Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency.
Muscular Atrophy
Glycolytic oligodendrocytes maintain myelin and long-term axonal integrity.
Muscular Diseases
Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency.
Nervous System Diseases
Oligomerization of Heme o Synthase in Cytochrome Oxidase Biogenesis Is Mediated by Cytochrome Oxidase Assembly Factor Coa2.
Neurodegenerative Diseases
A Targeted Mutation Disrupting Mitochondrial Complex IV Function in Primary Afferent Neurons Leads to Pain Hypersensitivity Through P2Y1 Receptor Activation.
Osteoporosis
Identification of B cells participated in the mechanism of postmenopausal women osteoporosis using microarray analysis.
Paralysis
Glycolytic oligodendrocytes maintain myelin and long-term axonal integrity.
Pulmonary Disease, Chronic Obstructive
Age-dependent assessment of genes involved in cellular senescence, telomere and mitochondrial pathways in human lung tissue of smokers, COPD and IPF: Associations with SARS-CoV-2 COVID-19 ACE2-TMPRSS2-Furin-DPP4 axis.
Pulmonary Disease, Chronic Obstructive
Age-Dependent Assessment of Genes Involved in Cellular Senescence, Telomere, and Mitochondrial Pathways in Human Lung Tissue of Smokers, COPD, and IPF: Associations With SARS-CoV-2 COVID-19 ACE2-TMPRSS2-Furin-DPP4 Axis.
Vascular System Injuries
RNA-sequencing reveals that STRN, ZNF484 and WNK1 add to the value of mitochondrial MT-COI and COX10 as markers of unstable coronary artery disease.
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the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
brenda
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malfunction
-
without this enzyme, Staphylococcus aureus is repressed in its ability to secrete cytolytic toxins
malfunction
-
deletion of the enzyme gene attenuates growth and virulence in mice but enhances pigment production and formation of quinolone tolerant persister cells in stationary phase
malfunction
-
without this enzyme, Staphylococcus aureus is repressed in its ability to secrete cytolytic toxins
-
malfunction
-
deletion of the enzyme gene attenuates growth and virulence in mice but enhances pigment production and formation of quinolone tolerant persister cells in stationary phase
-
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
metabolism
-
the enzyme is essential for processing heme into the electron transport chain for use as an electron acceptor
metabolism
-
the enzyme plays a role in heme A and heme O synthesis and seems to be required for both cytochrome a and cytochrome o synthesis
metabolism
-
the enzyme is essential for processing heme into the electron transport chain for use as an electron acceptor
-
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
-
physiological function
the assembly and activity of cytochrome c oxidase is dependent on the availability of heme A, one of its essential cofactors. In eukaryotes, two inner mitochondrial membrane proteins, heme O synthase (Cox10) and heme A synthase (Cox15), are required for heme A biosynthesis. The two physiological partners do not share the same regulatory mechanism. The stoichiometry between Cox15 and Cox10 is 8:1, not 1:1 as it has generally been assumed
physiological function
the enzyme catalyzes the first step in the conversion of protoheme to the heme A prosthetic groups of the cytochrome c oxidase
physiological function
-
the enzyme is involved in persister cell formation under stress and antibiotic treatment
physiological function
-
the assembly and activity of cytochrome c oxidase is dependent on the availability of heme A, one of its essential cofactors. In eukaryotes, two inner mitochondrial membrane proteins, heme O synthase (Cox10) and heme A synthase (Cox15), are required for heme A biosynthesis. The two physiological partners do not share the same regulatory mechanism. The stoichiometry between Cox15 and Cox10 is 8:1, not 1:1 as it has generally been assumed
-
physiological function
-
the enzyme is involved in persister cell formation under stress and antibiotic treatment
-
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?
-
x * 25000, SDS-PAGE
?
-
x * 32300, calculated from amino acid sequence
?
-
x * 33800, calculated from sequence
?
x * 28000, urea-SDS-PAGE
?
x * 34804, calculated from amino acid sequence
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
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
-
additional information
heme O synthase and heme A synthase interact and may form a physiologically relevant complex in vivo
additional information
-
heme O synthase and heme A synthase interact and may form a physiologically relevant complex in vivo
additional information
-
heme O synthase and heme A synthase interact and may form a physiologically relevant complex in vivo
-
additional information
heme O synthase and heme A synthase interact and may form a physiologically relevant complex in vivo
additional information
-
heme O synthase and heme A synthase interact and may form a physiologically relevant complex in vivo
additional information
-
heme O synthase and heme A synthase interact and may form a physiologically relevant complex in vivo
-
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C110A
catalytically active mutant enzyme
C54A
catalytically active mutant enzyme
D187A
nonfunctional enzyme
D256A
nonfunctional enzyme
D257A
nonfunctional enzyme
D282A
nonfunctional enzyme
D287A
catalytically active mutant enzyme
D61A
nonfunctional enzyme
D63A
nonfunctional enzyme
D65A
nonfunctional enzyme
F265A
catalytically active mutant enzyme
G139A
catalytically active mutant enzyme
G143A
nonfunctional enzyme
G150A
catalytically active mutant enzyme
G79A
catalytically active mutant enzyme
H131A
catalytically active mutant enzyme
H176A
nonfunctional enzyme
H207A
catalytically active mutant enzyme
K11A
nonfunctional enzyme
K129A
nonfunctional enzyme
K200A
catalytically active mutant enzyme
K206A
nonfunctional enzyme
L101A
catalytically active mutant enzyme
L232A
catalytically active mutant enzyme
L48A
catalytically active mutant enzyme
M68A
catalytically active mutant enzyme
N57A
nonfunctional enzyme
P146A
nonfunctional enzyme
P147A
catalytically active mutant enzyme
P175A
nonfunctional enzyme
R130A
catalytically active mutant enzyme
R70A
nonfunctional enzyme
R74A
nonfunctional enzyme
S268A
nonfunctional enzyme
T71A
catalytically active mutant enzyme
W172A
nonfunctional enzyme
Y120A
nonfunctional enzyme
Y124A
nonfunctional enzyme
Y1511A
nonfunctional enzyme
Y188A
nonfunctional enzyme
N204K
mutation causing COX-deficiency, disease-causing mutation, the mutant gene is not able to complement the yeast cox10 null strain when expressed in low copy
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
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
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
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
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
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
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
-
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
-
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
-
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
-
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
-
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Saiki, K.; Mogi, T.; Anraku, Y.
Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase
Biochem. Biophys. Res. Commun.
189
1491-1497
1993
Escherichia coli (P0AEA5), Escherichia coli
brenda
Brown, B.M.; Wang, Z.; Brown, K.R.; Cricco, J.A.; Hegg, E.L.
Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli
Biochemistry
43
13541-13548
2004
Bacillus subtilis (P24009), Bacillus subtilis, Cereibacter sphaeroides (Q3J5F9), Cereibacter sphaeroides, Bacillus subtilis 168 (P24009), Cereibacter sphaeroides DSM 158 (Q3J5F9)
brenda
Murakami, T.; Reiter, L.T.; Lupski, J.R.
Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene
Genomics
42
161-164
1997
Homo sapiens (Q12887), Homo sapiens
brenda
Valnot, I.; von Kleist-Retzow, J.C.; Barrientos, A.; Gorbatyuk, M.; Taanman, J.W.; Mehaye, B.; Rustin, P.; Tzagoloff, A.; Munnich, A.; Rtig, A.
A mutation in the human heme A:farnesyltransferase gene (COX10) causes cytochrome c oxidase deficiency
Hum. Mol. Genet.
9
1245-1249
2000
Homo sapiens (Q12887), Homo sapiens
brenda
Mogi T.
Over-expression and characterization of Bacillus subtilis heme O synthase
J. Biochem.
145
669-675
2009
Bacillus subtilis
brenda
Saiki, K.; Mogi, T.; Ogura, K.; Anraku, Y.
In vitro heme O synthesis by the cyoE gene product from Escherichia coli
J. Biol. Chem.
268
26041-26044
1993
Escherichia coli (P0AEA5), Escherichia coli
brenda
Saiki, K.; Mogi, T.; Hori, H.; Tsubaki, M.; Anraku, Y.
Identification of the functional domains in heme O synthase. Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli
J. Biol. Chem.
268
26927-16934
1993
Escherichia coli (P0AEA5), Escherichia coli
brenda
Wang, Z.; Wang, Y.; Hegg, E.L.
Regulation of the heme A biosynthetic pathway: differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae
J. Biol. Chem.
284
839-847
2009
Saccharomyces cerevisiae (P21592), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P21592)
brenda
Khalimonchuk, O.; Kim, H.; Watts, T.; Perez-Martinez, X.; Winge, D.R.
Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2
J. Biol. Chem.
287
26715-26726
2012
Saccharomyces cerevisiae (P21592), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P21592)
brenda
Glerum, D.M.; Tzagoloff, A.
Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant
Proc. Natl. Acad. Sci. USA
91
8452-8456
1994
Homo sapiens (Q12887), Homo sapiens
brenda
Malakhov, M.; Wada, H.; Los, D.; Murata, N.
The coxD gene for heme O synthase in Synechocystis
Biochim. Biophys. Acta
1273
84-86
1996
Synechocystis sp. PCC 6803 (Q55207)
brenda
Saiki, K.; Mogi, T.; Ishizuka, M.; Anraku, Y.
An Escherichia coli cyoE gene homologue in thermophilic Bacillus PS3 encodes a thermotolerant heme O synthase
FEBS Lett.
351
385-388
1994
Bacillus sp. PS3
brenda
Svensson, B.; Luebben, M.; Hederstedt, L.
Bacillus subtilis CtaA and CtaB function in haem A biosynthesis
Mol. Microbiol.
10
193-201
1993
Bacillus subtilis
brenda
Stevens, E.; Laabei, M.; Gardner, S.; Somerville, G.A.; Massey, R.C.
Cytolytic toxin production by Staphylococcus aureus is dependent upon the activity of the protoheme IX farnesyltransferase
Sci. Rep.
7
13744
2017
Staphylococcus aureus, Staphylococcus aureus JE2
brenda
Xu, T.; Han, J.; Zhang, J.; Chen, J.; Wu, N.; Zhang, W.; Zhang, Y.
Absence of protoheme IX farnesyltransferase CtaB causes virulence attenuation but enhances pigment production and persister survival in MRSA
Front. Microbiol.
7
1625
2019
Staphylococcus aureus, Staphylococcus aureus USA500
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