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Information on EC 2.5.1.141 - heme o synthase and Organism(s) Escherichia coli and UniProt Accession P0AEA5

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IUBMB Comments
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
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This record set is specific for:
Escherichia coli
UNIPROT: P0AEA5
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cox10, heme o synthase, heme a:farnesyltransferase, protoheme ix farnesyltransferase, cyoe protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CyoE protein
-
heme B farnesyltransferase
-
heme o synthase
-
JW0418
locus name
protoheme IX farnesyltransferase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:protoheme IX farnesyltranstransferase
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
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 SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
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+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dithionite
presence of reducing agents is essential, and dithionite is most effective among reagents tested
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
x * 26000, SDS-PAGE
28000
x * 28000, urea-SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team