HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.8.1.5 - 2-oxopropyl-CoM reductase (carboxylating)
Word Map on EC 1.8.1.5
- 1.8.1.5
- propylene
- disulfide
- thioether
- xanthobacter
- acetone
- autotrophicus
-
decarboxylation
- epoxide
- 2-bromoethanesulfonate
- epoxypropane
- co2
-
fad-containing
-
co2-fixing
-
air-oxidized
-
interchange
- flavin
-
fixation
- thiol
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: Xanthobacter
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.8.1.5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
2-oxopropyl-CoM reductase (carboxylating)
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-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
-
-
-
-
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
detailed reaction mechanism in a catalytic cycle, active site structure
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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
2-mercaptoethanesulfonate,acetoacetate:NADP+ oxidoreductase (decarboxylating)
Also acts on thioethers longer in chain length on the oxo side, e.g. 2-oxobutyl-CoM, but this portion must be attached to CoM (2-mercaptoethanesulfonate); no CoM analogs will substitute. This enzyme forms component II of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
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.
CAS REGISTRY NUMBER
COMMENTARY
244301-63-1
-
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
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-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + NADPH + H+
acetone + 2-mercaptoethanesulfonate + NADP+
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
3-mercaptopropionate + acetoacetate + NADP+
3-(2-oxopropylthio)propionate + CO2 + NADPH + H+
-
poor cofactor, 11% of activity
-
?
CO2 + acetoacetate
acetoacetate + CO2
-
exchange of C-14 without added cofactors
-
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
-
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
terminal enzyme in the metabolic pathway converting propylene to acetoacetate
-
-
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
i.e. 2-ketopropyl-CoM, comparison of enzyme structure with and without bound substrate, binding of 2-ketopropyl-coenzyme M induces a conformational change resulting in collapse of the substrate access channel, substrate binding site structure analysis
-
-
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
-
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
-
-
r
2-(2-oxopropylthio)ethanesulfonate + NADPH + H+
acetone + 2-mercaptoethanesulfonate + NADP+
-
-
-
ir
2-(2-oxopropylthio)ethanesulfonate + NADPH + H+
acetone + 2-mercaptoethanesulfonate + NADP+
-
-
-
ir
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
-
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
-
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
dual function enzyme, reverse reaction of component II of carboxylation pathway
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
dual function enzyme, reverse reaction of component II of carboxylation pathway
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
-
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
very poor cofactor, 1% of activity
-
?
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
very poor cofactor, 1% of activity
-
?
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-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
Q56839
terminal enzyme in the metabolic pathway converting propylene to acetoacetate
-
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
-
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-bromoethanesulfonate
-
reversible inhibitor, time-dependent inactivator of dithiothreitol-reduced 2-ketopropyl-CoM carboxylase/oxidoreductase, where the redox active cysteines are in the free thiol forms, does not inactivate air-oxidized 2-ketopropyl-CoM carboxylase/oxidoreductase, where the redox active cysteine pair is in the disulfide form. Inactivation leads to covalent modification of the interchange thiol residue C82. The flavin thiol Cys87 is not alkylated by 2-bromoethanesulfonate under reducing conditions, and no amino acid residues are modified by 2-bromoethanesulfonate in the oxidized enzyme
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
6.37
2-(2-oxopropylthio)ethanesulfonate
-
mutant M140A, pH 7.4, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.072
2-(2-oxopropylthio)ethanesulfonate
Xanthobacter autotrophicus
-
mutant M140A, pH 7.4, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
2-(2-oxopropylthio)ethanesulfonate
Xanthobacter autotrophicus
-
mutant M140A, pH 7.4, 30°C
7430
0.53
2-(2-oxopropylthio)ethanesulfonate
Xanthobacter autotrophicus
-
wild-type, pH 7.4, 30°C
7430
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.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme free or bound to substrate 2-ketopropyl-CoM, X-ray structure determination and analysis at 1.6-3.5 A resolution, multiple isomorphous replacement and anomalous scattering using four weak heavy atom derivatives
-
in complex with acetoacetate and 2-mercaptoethanesulfonate. In the substrate encapsulated state of the enzyme, CO2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H2O and prevents protonation of the ketopropyl leaving group
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C82A
-
mutagenesis of the interchange thiol, abolishes all redox-dependent reactions. Redox-independent acetoacetate decarboxylation is not decreased
C87A
-
mutagenesis of the flavin thiol, results in an inactive enzyme for steady-state redox-dependent reactions, but this variant catalyzes a single-turnover reaction producing a 0.8:1 ratio of product to enzyme. Redox-independent acetoacetate decarboxylation is not decreased
H137A
-
mutagenesis of the histidine proximal to the ordered water molecule, leads to nearly complete loss of redox-dependent reactions. Redox-independent acetoacetate decarboxylation is not decreased
H84A
-
mutagenesis of the distal histidine residue, reduces the redox-dependent activities by 58 to 76%. Redox-independent acetoacetate decarboxylation is not decreased
M140A
-
residue flanking the substrate, catalytic efficiency for 2-(2-oxopropylthio)ethanesulfonate carboxylation is 47fold lower than that for wild-type
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.
LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.5)
html completed
Information
