Information on EC 1.8.1.5 - 2-oxopropyl-CoM reductase (carboxylating)

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The expected taxonomic range for this enzyme is: Xanthobacter

EC NUMBER
COMMENTARY hide
1.8.1.5
-
RECOMMENDED NAME
GeneOntology No.
2-oxopropyl-CoM reductase (carboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
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redox reaction
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-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethene and chloroethene degradation
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propene degradation
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-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
244301-63-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Py2
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
show the reaction diagram
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
show the reaction diagram
2-(2-oxopropylthio)ethanesulfonate + NADPH + H+
acetone + 2-mercaptoethanesulfonate + NADP+
show the reaction diagram
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
show the reaction diagram
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
show the reaction diagram
3-mercaptopropionate + acetoacetate + NADP+
3-(2-oxopropylthio)propionate + CO2 + NADPH + H+
show the reaction diagram
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poor cofactor, 11% of activity
-
?
acetoacetate + H+
acetone + CO2
show the reaction diagram
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very low rate
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?
CO2 + acetoacetate
acetoacetate + CO2
show the reaction diagram
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exchange of C-14 without added cofactors
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?
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
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
show the reaction diagram
Q56839
terminal enzyme in the metabolic pathway converting propylene to acetoacetate
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-
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanesulfonic acid
-
coenzyme M
NADP+
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binding domain structure analysis
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-bromoethanesulfonate
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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
N-ethylmaleimide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.42 - 6.37
2-(2-oxopropylthio)ethanesulfonate
6.3
acetoacetate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072 - 0.22
2-(2-oxopropylthio)ethanesulfonate
0.263
acetoacetate
Xanthobacter sp.
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 0.53
2-(2-oxopropylthio)ethanesulfonate
7430
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0041
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rate of decarboxylation without added cofactors
0.274
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NADPH formation
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
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molecular weight of subunits
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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hanging drop vapour diffusion method
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C82A
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mutagenesis of the interchange thiol, abolishes all redox-dependent reactions. Redox-independent acetoacetate decarboxylation is not decreased
C87A
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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
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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
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mutagenesis of the distal histidine residue, reduces the redox-dependent activities by 58 to 76%. Redox-independent acetoacetate decarboxylation is not decreased
M140A
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residue flanking the substrate, catalytic efficiency for 2-(2-oxopropylthio)ethanesulfonate carboxylation is 47fold lower than that for wild-type