Information on EC 4.4.1.23 - 2-hydroxypropyl-CoM lyase

New: Word Map on EC 4.4.1.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.4.1.23
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxypropyl-CoM lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM
show the reaction diagram
-
-
-
-
(S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-S bond cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethene and chloroethene degradation
-
-
propene degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)
Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I 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
244301-07-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JS60
-
-
Manually annotated by BRENDA team
strain JS60
-
-
Manually annotated by BRENDA team
variant JS 623-E and JS 623-T
UniProt
Manually annotated by BRENDA team
strain JS614
-
-
Manually annotated by BRENDA team
strain TD
-
-
Manually annotated by BRENDA team
strain TD
-
-
Manually annotated by BRENDA team
strain AJ
-
-
Manually annotated by BRENDA team
strain AJ
-
-
Manually annotated by BRENDA team
B276
-
-
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-hydroxypropyl-CoM
1,2-epoxypropane + HS-CoM
show the reaction diagram
-
-
-
-
?
epoxyethane + CoM
2-hydroxyethyl-CoM
show the reaction diagram
assay at pH 8.0, 30C
-
-
?
epoxyethane + HS-CoM
2-hydroxyethyl-CoM
show the reaction diagram
epoxypropane + 3-mercaptopropionate
3-[(2-hydroxypropyl)thio]propanoic acid
show the reaction diagram
-
0.59% of the activity with HS-CoM
-
-
?
epoxypropane + HS-CoA
?
show the reaction diagram
epoxypropane + HS-CoM
2-hydroxypropyl-CoM
show the reaction diagram
ethene + HS-CoM
?
show the reaction diagram
ethylene oxide + HS-CoM
?
show the reaction diagram
vinyl chloride + HS-CoM
?
show the reaction diagram
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
epoxypropane + HS-CoM
2-hydroxypropyl-CoM
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2
Zn
-
Zn plays a key role in activating an organic thiol substrate for nucleophilic attack on an alkyl-donating substrate, removal of Zn results in loss of catalytic activity, the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2. Thermodynamic characterization of the interaction of CoM with an enzyme-bound Zn center
Zn2+
-
the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
weak competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018
epoxypropane
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.5
epoxypropane
Xanthobacter autotrophicus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.039
wild-type enzyme, transferred to Mycobacterium smegmatis; wild-type enzyme, transferred to Mycobacterium smegmatis
0.056
mutation W243G, transferred to Mycobacterium smegmatis; mutation W243G, transferred to Mycobacterium smegmatis
0.062
mutation R257L, transferred to Mycobacterium smegmatis; mutation R257L, transferred to Mycobacterium smegmatis
0.074
wild-type enzyme; wild-type enzyme
0.15
vinyl-chloride adapted variant JS623-E; vinyl-chloride adapted variant JS623-E
0.645
vinyl-chloride adapted variant JS623-T; vinyl-chloride adapted variant JS623-T
1.3
-
substrate ethylene oxide, 30C
3.4
-
substrate ethene, 30C
3.5
-
substrate ethylene oxide, 30C
3.7
-
substrate vinyl chloride, 30C
4.4
-
substrate vinyl chloride, 30C
4.6
-
substrate ethene, 30C
143
-
epoxypropane as substrate
615
-
epoxyethane as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
-
pH 7.0: about 85% of maximal activity, pH 9.5: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
this enzyme forms component I of a four-component enzyme system, comprising EC 4.2.99.19 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 II and EC 1.1.1.269 2-(S)-hydroxypropyl-CoM dehydrogenase, component IV that is involved in epoxyalkane carboxylation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Mycobacterium smegmatis
-
expression in Escherichia coli
-
expression in Escherichia coli and Mycobacterium smegmatis; expression in Escherichia coli and Mycobacterium smegmatis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R257L
higher enzyme activities compared to wild-type, growth on vinyl chloride more rapidly than the wild-type strain; higher enzyme activities compared to wild-type, growth on vinyl chloride more rapidly than the wild-type strain
W243G
higher enzyme activities compared to wild-type, growth on vinyl chloride more rapidly than the wild-type strain; higher enzyme activities compared to wild-type, growth on vinyl chloride more rapidly than the wild-type strain
C220A
-
largely catalytically inactive protein, 0.06% of wild-type activity
additional information