HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 6.4.1.8 - acetophenone carboxylase
for references in articles please use BRENDA:EC6.4.1.8
Word Map on EC 6.4.1.8
- 6.4.1.8
-
aromatoleum
- aromaticum
- ethylbenzene
- acetone
-
denitrifying
-
polyproline
- atpase
-
betaproteobacterium
- zn
-
ii-like
-
bundle
-
s-1-phenylethanol
-
petroleum
- bicarbonate
- bal
- analysis
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Aromatoleum aromaticum
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
6.4.1.8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
acetophenone carboxylase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ATP + acetophenone + HCO3- + H2O + H+ = 2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acetophenone:carbon-dioxide ligase (ADP-forming)
The enzyme is involved in anaerobic degradation of ethylbenzene. No activity with acetone, butanone, 4-hydroxy-acetophenone or 4-amino-acetophenone.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q5P5G2 i.e. alpha-subunit, Q5P5G3 i.e. beta-subunit, Q5P5G4 i.e. gamma-subunit, Q5P5G5 i.e. delta-subunit, Q5P5G6 i.e. epsilon-subunit
UniProt
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ATP + 4-acetylpyridine + HCO3- + H2O + H+
2 ADP + 2 phosphate + 2-oxo-3-(pyridin-4-yl)propanoate
2 ATP + 4-acetylpyridine + HCO3- + H2O + H+
2 ADP + 2 phosphate + 2-oxo-3-(pyridin-4-yl)propanoate
-
22% of the activity with acetophenone
-
-
?
2 ATP + 4-acetylpyridine + HCO3- + H2O + H+
2 ADP + 2 phosphate + 2-oxo-3-(pyridin-4-yl)propanoate
-
22% of the activity with acetophenone
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
-
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
anaerobic ethylbenzene metabolism in the betaproteobacterium Aromatoleum aromaticum is initiated by anaerobic oxidation to acetophenone via (S)-1-phenylethanol. The subsequent carboxylation of acetophenone to benzoylacetate is catalyzed by an acetophenone-induced enzyme
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
the enzyme shows uncoupled ATPase activity with either bicarbonate or acetophenone in the absence of the second substrate. These observations indicate that both substrates may be phosphorylated. Purified enzyme shows no activity with GTP, CTP, UTP or ITP
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
-
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
anaerobic ethylbenzene metabolism in the betaproteobacterium Aromatoleum aromaticum is initiated by anaerobic oxidation to acetophenone via (S)-1-phenylethanol. The subsequent carboxylation of acetophenone to benzoylacetate is catalyzed by an acetophenone-induced enzyme
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
the enzyme shows uncoupled ATPase activity with either bicarbonate or acetophenone in the absence of the second substrate. These observations indicate that both substrates may be phosphorylated. Purified enzyme shows no activity with GTP, CTP, UTP or ITP
-
-
?
2 ATP + propiophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 4-oxo-4-phenylbutanoate
-
108% of the activity with acetophenone
-
-
?
2 ATP + propiophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 4-oxo-4-phenylbutanoate
-
108% of the activity with acetophenone
-
-
?
additional information
?
-
-
no activity with acetone, butanone, 4-hydroxy-acetophenone or 4-amino-acetophenone
-
-
-
additional information
?
-
-
no activity with acetone, butanone, 4-hydroxy-acetophenone or 4-amino-acetophenone
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
anaerobic ethylbenzene metabolism in the betaproteobacterium Aromatoleum aromaticum is initiated by anaerobic oxidation to acetophenone via (S)-1-phenylethanol. The subsequent carboxylation of acetophenone to benzoylacetate is catalyzed by an acetophenone-induced enzyme
-
-
?
2 ATP + acetophenone + HCO3- + H2O + H+
2 ADP + 2 phosphate + 3-oxo-3-phenylpropanoate
-
anaerobic ethylbenzene metabolism in the betaproteobacterium Aromatoleum aromaticum is initiated by anaerobic oxidation to acetophenone via (S)-1-phenylethanol. The subsequent carboxylation of acetophenone to benzoylacetate is catalyzed by an acetophenone-induced enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
-
the enzyme contains 1 Zn2+ ion per alphabetagammadelta core complex. In spite of the presence of Zn in the enzyme, it is strongly inhibited by Zn2+ ions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta,gamma-Imido-ATP
-
2 mM, complete inhibition of acetophenone carboxylase activity, non-competitive inhibition
Carbamoyl phosphate
-
2 mM: 50% inhibition of ATPase activity. 8 mM: 50% inhibition of carboxylating activity
Ni2+
-
1 mM: 50% inhibition of ATPase activity. 2.5 mM: 50% inhibition of carboxylation activity
Zn2+
-
the enzyme contains 1 Zn2+ ion per alphabetagammadelta core complex. In spite of the presence of Zn in the enzyme, it is strongly inhibited by Zn2+ ions. 0.2 mM ZnCl2: 50% inhibition of ATPase activity and carboxylation activity
additional information
-
acetophenone carboxylation activity in cell extracts is not sensitive to avidin, indicating that the enzyme is independent of biotin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15000
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
34000
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
70000
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
75000
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
87000
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentamer
pentamer
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
pentamer
-
1 * 70000 (alpha) + 1 * 15000 (beta) + 1 * 87000 (gamma) + 1 * 75000 (delta) + 1 * 34000 (epsilon), the genes (apcABCDE) of the five subunits form an apparent operon
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of the Apc(alphaalpha'betagamma)2 core complex, to 3.0 A resolution. Subunit Apcbeta contains a domain fold composed of two beta-sheets in a barrel-like arrangement running into a bundle of eight short polyproline (type II)-like helical segments. Apcalpha and Apcalpha' possess ATP-binding modules of the ASKHA superfamily and presumably operate as ATP-dependent kinases for acetophenone and bicarbonate, respectively
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
during purification, acetophenone carboxylase dissociates into inactive subcomplexes consisting of the 70-, 15-, 87-, and 75-kDa subunits (apcABCD gene products) and the 34-kDa subunit (apcE gene product), respectively. Acetophenone carboxylase activity is restored by mixing the purified subcomplexes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterologous expression of the apcEC-His6 subunit in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
acetophenone carboxylase is formed in ethylbenzene- and toluene-adapted cells
-
acetophenone carboxylase is formed in ethylbenzene- and toluene-adapted cells; expression of alpha-subunit is proportional to the applied acetophenone concentrations; the enzyme is synthesized at high levels in cells grown on ethylbenzene or acetophenone, but not in cells grown on benzoate
-
-
expression of alpha-subunit is proportional to the applied acetophenone concentrations
-
the enzyme is synthesized at high levels in cells grown on ethylbenzene or acetophenone, but not in cells grown on benzoate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
construction of a reporter strain by inserting a gene fusion of apcA, the first gene of the apc-bal operon, with the gene for the fluorescent protein mCherry into the chromosome. mCherry production is proportional to the applied acetophenone concentrations. The reporter strain allows quantification of acetophenone within a concentration range of 50 microM (detection limit) to 250 microM after 12 and 24 h. Production of the Apc-mCherry fusion protein in the reporter strain is highly specific and responds to acetophenone and both enantiomers of 1-phenylethanol
analysis
-
construction of a reporter strain by inserting a gene fusion of apcA, the first gene of the apc-bal operon, with the gene for the fluorescent protein mCherry into the chromosome. mCherry production is proportional to the applied acetophenone concentrations. The reporter strain allows quantification of acetophenone within a concentration range of 50 microM (detection limit) to 250 microM after 12 and 24 h. Production of the Apc-mCherry fusion protein in the reporter strain is highly specific and responds to acetophenone and both enantiomers of 1-phenylethanol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 6.4.1.8)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
