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Information on EC 1.8.1.5 - 2-oxopropyl-CoM reductase (carboxylating)
for references in articles please use BRENDA:EC1.8.1.5
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.1 With NAD+ or NADP+ as acceptor
1.8.1.5 2-oxopropyl-CoM reductase (carboxylating)
IUBMB Comments
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-sulfanylethane-1-sulfonate); no CoM analogs will substitute. This enzyme forms component II of a four-component enzyme system 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].html">click here that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
The enzyme appears in viruses and cellular organisms
- 1.8.1.5
- propylene
- thioether
- co2
- acetone
- xanthobacter
- flavin
- 2-bromoethanesulfonate
-
dyad
-
co2-fixing
-
fad-containing
- epoxypropane
- epoxide
- autotrophicus
-
phe-his
- pka
-
electrophile
- thioredoxins
- his-glu
-
interchange
-
encapsulate
-
air-oxidized
Reaction Schemes
showSynonyms
2-kpcc, nadph:2-ketopropyl-coenzyme m oxidoreductase/carboxylase, 2-ketopropyl-coenzyme m oxidoreductase/carboxylase, 2-ketopropyl coenzyme m oxidoreductase/carboxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-ketopropyl coenzyme M oxidoreductase/carboxylase
-
2-KPCC
NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase
-
-
-
-
NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase
additional information
enzyme belongs to the disulfide oxidoreductase family of enzymes DSOR
NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
-
-
-
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
detailed reaction mechanism in a catalytic cycle, active site structure
2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
reaction mechanism for 2-KPCC begins with formation of enzyme-substrate disulfide adduct by the reduced form of the redox active disulfide. This step is followed by release of enolacetone anion intermediates for 2-KPCC. The primary catalytic fate of the enolacetone intermediate for the wild-type (Phe501) or variant (His501) 2-KPCC is acetoacetate or acetone, respectively
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
ethene and chloroethene degradation, 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-sulfanylethane-1-sulfonate); 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.
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CAS REGISTRY NUMBER
COMMENTARY
244301-63-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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+
2-oxopropyl-coenzyme M + CO2 + NADPH
coenzyme M + acetoacetate + NADP+
Substrates: -
Products: -
Products: -
?
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
3-mercaptopropionate + acetoacetate + NADP+
3-(2-oxopropylthio)propionate + CO2 + NADPH + H+
-
Substrates: poor cofactor, 11% of activity
Products: -
Products: -
?
CO2 + acetoacetate
acetoacetate + CO2
-
Substrates: exchange of C-14 without added cofactors
Products: -
Products: -
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
Substrates: -
Products: -
Products: -
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
Substrates: terminal enzyme in the metabolic pathway converting propylene to acetoacetate
Products: -
Products: -
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
Substrates: 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
Products: -
Products: -
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
Substrates: -
Products: -
Products: -
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-mercaptoethanesulfonate + acetoacetate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-(2-oxopropylthio)ethanesulfonate + NADPH + H+
acetone + 2-mercaptoethanesulfonate + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-(2-oxopropylthio)ethanesulfonate + NADPH + H+
acetone + 2-mercaptoethanesulfonate + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: dual function enzyme, reverse reaction of component II of carboxylation pathway
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: dual function enzyme, reverse reaction of component II of carboxylation pathway
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
Products: -
Products: -
r
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: very poor cofactor, 1% of activity
Products: -
Products: -
?
3-mercaptopropanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: very poor cofactor, 1% of activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
2-oxopropyl-coenzyme M + CO2 + NADPH
coenzyme M + acetoacetate + NADP+
Substrates: -
Products: -
Products: -
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
Substrates: -
Products: -
Products: -
?
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH
2-mercaptoethanesulfonate + acetoacetate + NADP+
Substrates: terminal enzyme in the metabolic pathway converting propylene to acetoacetate
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
Products: -
Products: -
r
2-mercaptoethanesulfonate + acetoacetate + NADP+
2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH + H+
-
Substrates: involved in epoxide carboxylation pathway in bacteria, reverse reaction more important
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.42
2-(2-oxopropylthio)ethanesulfonate
wild-type, pH 7.4, 30Ā°C
6.37
2-(2-oxopropylthio)ethanesulfonate
mutant M140A, pH 7.4, 30Ā°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.072
2-(2-oxopropylthio)ethanesulfonate
mutant M140A, pH 7.4, 30Ā°C
0.22
2-(2-oxopropylthio)ethanesulfonate
wild-type, pH 7.4, 30Ā°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
2-(2-oxopropylthio)ethanesulfonate
mutant M140A, pH 7.4, 30Ā°C
0.53
2-(2-oxopropylthio)ethanesulfonate
wild-type, pH 7.4, 30Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the disulfide oxidoreductase (DSOR) family of enzymes. The characteristic His-Glu catalytic dyad of the DSOR family is replaced in 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) uniquely by the residues Phe-His, potentially to eliminate proton-donating groups at a key position in the active site. These differences in 2-KPCC are key in discriminating between carbon dioxide and protons as attacking electrophiles
physiological function
2-oxopropylcoenzyme M oxidoreductase/carboxylase (2-KPCC) catalyzes the reductive cleavage and carboxylation of 2-oxopropyl coenzyme M (2-KPC) to form acetoacetate and concomitantly regenerate CoM (2-mercaptoethanesulfonate)
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). XECC_XANP2
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
523
0
57348
Swiss-Prot
-
A7IQH7_XANP2
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
130
0
14381
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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
vapor diffusion method, using 0.17 M ammonium acetate, 0.085 M trisodium citrate, pH 5.6, 27% (w/v) PEG 4000, and 15% (v/v) glycerol
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PROTEIN VARIANTS
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
F501H
the mutant shows 10% acetoacetate production activity compared to the wild type enzyme. The overall rate of NADPH turnover remains relatively unchanged in the F501H variant relative to wild type. Moreover, acetone formation by F501H is comparable in rate to the carboxylation reaction catalyzed by wild type enzyme and leading to acetoacetate
F501H/H506E
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
H506E
the mutant shows 37% acetoacetate production activity compared to the wild type enzyme. NADPH turnover is around 1.5fold slower in H506E versus wild type enzyme
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
F501H/H506E
site-directed mutagenesis of the catalytic dyad, substitution of the Phe-His active site residues by the canonical residues results in production of higher relative concentrations of acetone versus the natural product acetoacetate. Replacement of the His-Glu dyad from DSORs with Phe-His is critical for specifying carboxylation chemistry in enzyme 2-KPCC
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography, and DEAE-Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS or BL21(DE3) cells
recombinant expression of wild-type and mutant enzymes in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allen, J.R.; Clark, D.D.; Krum, J.G.; Ensign, S.A.
A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation
Proc. Natl. Acad. Sci. USA
96
8432-8437
1999
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Clark, D.D.; Allen, J.R.; Ensign, S.A.
Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system
Biochemistry
39
1294-1304
2000
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Jang, S.B.; Jeong, M.S.; Clark, D.D.; Ensign, S.A.; Peters, J.W.
Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase
Acta Crystallogr. Sect. D
57
445-447
2001
Xanthobacter sp.
brenda
Nocek, B.; Jang, S.B.; Jeong, M.S.; Clark, D.D.; Ensign, S.A.; Peters, J.W.
Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase
Biochemistry
41
12907-12913
2002
Xanthobacter autotrophicus (Q56839)
brenda
Pandey, A.S.; Nocek, B.; Clark, D.D.; Ensign, S.A.; Peters, J.W.
Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase
Biochemistry
45
113-120
2006
Xanthobacter autotrophicus (Q56839)
brenda
Boyd, J.M.; Clark, D.D.; Kofoed, M.A.; Ensign, S.A.
Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate
J. Biol. Chem.
285
25232-25242
2010
Xanthobacter autotrophicus
brenda
Pandey, A.S.; Mulder, D.W.; Ensign, S.A.; Peters, J.W.
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase
FEBS Lett.
585
459-464
2011
Xanthobacter autotrophicus (Q56839)
brenda
Kofoed, M.A.; Wampler, D.A.; Pandey, A.S.; Peters, J.W.; Ensign, S.A.
Roles of the redox-active disulfide and histidine residues forming a catalytic dyad in reactions catalyzed by 2-ketopropyl coenzyme M oxidoreductase/carboxylase
J. Bacteriol.
193
4904-4913
2011
Xanthobacter autotrophicus (Q56839)
brenda
Prussia, G.A.; Gauss, G.H.; Mus, F.; Conner, L.; DuBois, J.L.; Peters, J.W.
Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity
FEBS Lett.
590
2991-2996
2016
Xanthobacter autotrophicus (Q56839)
brenda
Streit, B.R.; Mattice, J.R.; Prussia, G.A.; Peters, J.W.; DuBois, J.L.
The reactive form of a C-S bond-cleaving, CO2-fixing flavoenzyme
J. Biol. Chem.
294
5137-5145
2019
Xanthobacter autotrophicus (Q56839)
brenda
Prussia, G.A.; Shisler, K.A.; Zadvornyy, O.A.; Streit, B.R.; DuBois, J.L.; Peters, J.W.
The unique Phe-His dyad of 2-ketopropyl coenzyme M oxidoreductase/carboxylase selectively promotes carboxylation and S-C bond cleavage
J. Biol. Chem.
297
100961
2021
Xanthobacter autotrophicus (Q56839)
brenda
EXTERNAL LINKS (specific for EC-Number 1.8.1.5)
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