Information on EC 2.5.1.B36 - protoheme IX farnesyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.5.1.B36
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
protoheme IX farnesyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O = heme o + diphosphate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
protoheme IX:(2E,6E)-farnesyl diphosphate farnesyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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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+
Mg2+
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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+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithionite
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presence of reducing agents is essential, and dithionite is most effective among reagents tested
additional information
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Cox10 is not affected by the presence/absence of its physiological partner, Cox15
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
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the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
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the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
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the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
-
the gene is expressed in multiple tissues with highest expression observed in the heart, skeletal muscle, and testis
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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x * 26000, SDS-PAGE
28000
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x * 28000, urea-SDS-PAGE
33800
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x * 33800, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the stability of Cox10 is not decreased in the absence of cytochrome c oxidase
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed of 6 * His epitope-tagged enzyme in Escherichia coli
overexpression of His7-tagged enzymee in Escherichia. coli
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the human COX10 homolog does not complement the mutation of a yeast cox10 null mutant as efficiently as the yeast COX10 protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
COX10 is regulated neither by intracellular heme B levels nor by Hap1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C110A
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catalytically active mutant enzyme
C54A
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catalytically active mutant enzyme
D187A
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nonfunctional enzyme
D256A
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nonfunctional enzyme
D257A
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nonfunctional enzyme
D282A
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nonfunctional enzyme
D287A
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catalytically active mutant enzyme
D61A
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nonfunctional enzyme
D63A
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nonfunctional enzyme
D65A
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nonfunctional enzyme
F265A
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catalytically active mutant enzyme
G139A
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catalytically active mutant enzyme
G143A
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nonfunctional enzyme
G150A
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catalytically active mutant enzyme
G79A
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catalytically active mutant enzyme
H131A
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catalytically active mutant enzyme
H176A
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nonfunctional enzyme
H207A
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catalytically active mutant enzyme
K11A
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nonfunctional enzyme
K129A
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nonfunctional enzyme
K200A
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catalytically active mutant enzyme
K206A
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nonfunctional enzyme
L101A
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catalytically active mutant enzyme
L232A
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catalytically active mutant enzyme
L48A
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catalytically active mutant enzyme
M68A
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catalytically active mutant enzyme
N57A
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nonfunctional enzyme
P146A
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nonfunctional enzyme
P147A
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catalytically active mutant enzyme
P175A
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nonfunctional enzyme
R130A
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catalytically active mutant enzyme
R70A
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nonfunctional enzyme
R74A
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nonfunctional enzyme
S268A
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nonfunctional enzyme
T71A
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catalytically active mutant enzyme
W172A
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nonfunctional enzyme
Y120A
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nonfunctional enzyme
Y124A
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nonfunctional enzyme
Y1511A
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nonfunctional enzyme
Y188A
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nonfunctional enzyme
D282A
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nonfunctional enzyme
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G79A
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catalytically active mutant enzyme
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H131A
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catalytically active mutant enzyme
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P175A
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nonfunctional enzyme
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T71A
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catalytically active mutant enzyme
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N204K
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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
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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
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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
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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
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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
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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
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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
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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
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E328G
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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
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E328V
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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
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P217L
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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
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T188K
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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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