Information on EC 5.5.1.1 - Muconate cycloisomerase

for references in articles please use BRENDA:EC5.5.1.1
Word Map on EC 5.5.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.5.1.1
-
RECOMMENDED NAME
GeneOntology No.
Muconate cycloisomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,5-Dihydro-5-oxofuran-2-acetate = cis,cis-hexadienedioate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,2-elimination
-
-
-
-
4,5-elimination
-
-
-
-
cyclization
-
-
intramolecular
-
elimination/addition
-
-
intramolecular
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
catechol degradation to beta-ketoadipate
-
-
phenol degradation
-
-
Chlorocyclohexane and chlorobenzene degradation
-
-
Benzoate degradation
-
-
Fluorobenzoate degradation
-
-
Toluene degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
2,5-Dihydro-5-oxofuran-2-acetate lyase (decyclizing)
Requires Mn2+. Also acts (in the reverse reaction) on 3-methyl-cis,cis-muconate and, very slowly, on cis,trans-muconate. Not identical with EC 5.5.1.7 (chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).
CAS REGISTRY NUMBER
COMMENTARY hide
9023-72-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
335; basonym Alcaligenes eutrophus; JMP134
-
-
Manually annotated by BRENDA team
CA28
-
-
Manually annotated by BRENDA team
CA28
-
-
Manually annotated by BRENDA team
Frateuria sp.
ANA-18
-
-
Manually annotated by BRENDA team
ANA-18
-
-
Manually annotated by BRENDA team
GJ31
-
-
Manually annotated by BRENDA team
WR1323
-
-
Manually annotated by BRENDA team
isoform SalC
SwissProt
Manually annotated by BRENDA team
B13
-
-
Manually annotated by BRENDA team
isoform CatB
-
-
Manually annotated by BRENDA team
RHO1
-
-
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
2,3-dimethyl-cis,cis-muconate
2,3-dimethylmuconolactone
show the reaction diagram
-
-
-
?
2,4-dichloro-cis,cis-muconate
?
show the reaction diagram
2,4-dimethyl-cis,cis-muconate
2,4-dimethylmuconolactone
show the reaction diagram
-
-
-
?
2-chloro-cis,cis-muconate
(+)-2-chloromuconolactone + (+)-5-chloromuconolactone
show the reaction diagram
-
-
mutant enzymes I54V and I54V/Y59W form 5-chloromuconolactone almost exclusively. Mutant enzymes F329I and Y59W form 2-chloromuconolactone as the main product. Mutant enzyme A271S hehaves similar to wild-type enzyme
?
2-chloro-cis,cis-muconate
5-chloromuconolactone + 2-chloromuconolactone
show the reaction diagram
2-Chloro-cis,cis-muconate
?
show the reaction diagram
2-methyl-cis,cis-muconate
2-methylmuconolactone
show the reaction diagram
2-Methyl-cis,cis-muconate
?
show the reaction diagram
2-methylmuconate
?
show the reaction diagram
3-Bromo-cis,cis-muconate
?
show the reaction diagram
-
at 9% of the activity relative to 3-methyl-cis,cis-muconate
-
-
-
3-chloro-cis,cis-muconate
4-chloro-muconolactone
show the reaction diagram
3-Chloro-cis,cis-muconate
5-Chloromuconolactone
show the reaction diagram
3-chloro-cis,cis-muconate
?
show the reaction diagram
-
-
?
3-chloro-cis,cis-muconate
cis-dienelactone + protoanemonin + Cl- + H2O + CO2
show the reaction diagram
3-chloro-cis,cis-muconate
protoanemonin + ?
show the reaction diagram
-
-
formed by wild-type enzyme and mutant enzymes I54V, A271S, K276N, F329I, L333V, I54V/F329I
?
3-chloromuconate
?
show the reaction diagram
3-chloromuconate
cis-dienelactone + protoanemonin
show the reaction diagram
the highest turnover rate, 10fold higher than with 3-methylmuconate, is observed with 3-chloromuconate
-
-
?
3-ethyl-cis,cis-muconate
4-ethylmuconolactone
show the reaction diagram
3-Fluoro-cis,cis-muconate
(+)-4-Fluoromuconolactone
show the reaction diagram
3-Fluoro-cis,cis-muconate
?
show the reaction diagram
3-methyl-cis,cis-muconate
4-methylmuconolactone
show the reaction diagram
3-Methyl-cis,cis-muconate
?
show the reaction diagram
3-Methyl-cis,cis-muconate
beta-Methylmuconolactone
show the reaction diagram
3-methylmuconate
?
show the reaction diagram
cis,cis-hexadienedioate
2,5-dihydro-5-oxofuran-2-acetate
show the reaction diagram
cis,cis-muconate
(+)-(4S)-muconolactone
show the reaction diagram
-
syn-cycloisomerization
-
-
?
cis,cis-Muconate
(+)-Muconolactone
show the reaction diagram
cis,cis-muconate
(4S)-muconolactone
show the reaction diagram
cis,cis-Muconate
?
show the reaction diagram
cis,cis-muconate
muconolactone
show the reaction diagram
cis,trans-Muconate
?
show the reaction diagram
3-chloro-cis,cis-muconate
additional information
-
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
3-Methyl-cis,cis-muconate
?
show the reaction diagram
-
enzyme of the beta-ketoadipate pathway that also functions in the reaction sequence for converting 3-methyl-cis,cis-muconate
-
-
-
cis,cis-Muconate
?
show the reaction diagram
cis,cis-muconate
muconolactone
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
Frateuria sp.
-
0.4% of the activity with Mn2+, enzyme form MC II
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-dichloro-cis,cis-muconate
2-fluoro-cis,cis-muconate
3-chloro-cis,cis-muconate
-
inhibitor of cis,cis-muconate conversion
CuSO4
HgCl2
nitriloacetic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026 - 0.093
2,4-dichloro-cis,cis-muconate
0.017 - 0.415
2-chloro-cis,cis-muconate
0.029 - 0.49
2-methyl-cis,cis-muconate
0.04
2-methylmuconate
-
0.045 - 1.24
3-chloro-cis,cis-muconate
0.105
3-chloromuconate
-
0.67
3-ethyl-cis,cis-muconate
-
24°C, pH 8.0
0.063 - 0.23
3-fluoro-cis,cis-muconate
0.006 - 0.099
3-methyl-cis,cis-muconate
0.0106
3-methylmuconate
-
0.0071 - 1.73
cis,cis-muconate
0.424
muconolactone
-
-
additional information
additional information
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 72000
2,4-dichloro-cis,cis-muconate
3.6 - 2940
2-chloro-cis,cis-muconate
3 - 600000
2-methyl-cis,cis-muconate
0.5
2-methylmuconate
-
8.8 - 57600
3-chloro-cis,cis-muconate
111
3-chloromuconate
-
156000 - 534000
3-fluoro-cis,cis-muconate
2 - 108000
3-methyl-cis,cis-muconate
11
3-methylmuconate
-
4 - 756000
cis,cis-muconate
1.4
muconolactone
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
2-methylmuconate
-
1100
3-chloromuconate
-
1000
3-methylmuconate
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035 - 0.035
2,4-dichloro-cis,cis-muconate
0.027 - 0.031
2-fluoro-cis,cis-muconate
0.095
3-chloro-cis,cis-muconate
-
inhibitor of cis,cis-muconate conversion
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.017
-
substrate 3-chloro-cis,cis-muconate, crude enzyme extrat
0.035
-
substrate cis,cis-muconate, crude enzyme extract
0.49
-
cell-free extract
8.3
-
after 17fold purification
41
-
24°C, pH 8.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
Frateuria sp.
-
enzyme form MC I and MC II
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2 - 6.5
-
50% of maximal activity at pH 3.2 and 6.5
5.5 - 7.5
Frateuria sp.
-
enzyme form MCI shows more than 80% of maximal activity in the range pH 5.5-7.5
6 - 7
-
less than 50% of maximal activity below pH 6 and above pH 7
6 - 8.5
-
pH 6: about 60% of maximal activity, pH 8.5: about 50% of maximal activity
6 - 7
Frateuria sp.
-
enzyme form MCII shows more than 80% of maximal activity in the range pH 6.0-7.0
6 - 8
-
about 65% of maximal activity at pH 6 and pH 8
7 - 11
-
more than 70% of maximum activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39760
subunit, calculated from amino acid sequence
40248
x * 40248, calculated
40926
-
6 * 43000, SDS-PAGE, 6 * 40926, calculated
41076
-
x * 41076, calculated, x * 42000, SDS-PAGE
44000
Frateuria sp.
-
x * 44000, SDS-PAGE
48000
-
1 * 48000, SDS-PAGE
52000
-
gel filtration
169000
-
gel filtration
230000 - 250000
-
nondenaturing electrophoresis, gel filtration
236000
-
gel filtration
248500 - 260000
-
sedimentation equilibrium studies, gel filtration
280000
-
gel filtration
350000
gel filtration
400000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homooctamer
monomer
-
1 * 48000, SDS-PAGE
octamer
-
8 * 40000
tetramer
-
4 * 43000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with Mg2+, hanging drop vapor diffusion method, using 10% (v/v) 2-propanol, 0.1 M MES, pH 6.0, and 0.2 M Ca(OAc)2, or in complex with Mg2+ and cis,cis-muconate, hanging drop vapor diffusion method, using 1.0 M (NH4)2SO4, 0.1 M HEPES, pH 7.0, and 0.5% (w/v) PEG 8000
-
in complex with Mg2+, hanging drop vapor diffusion method, using 20% (v/v) PEG 1000, 0.1 M cacodylate, pH 6.5, and 0.2 M MgCl2, or in complex with Mg2+ and cis,cis-muconate, hanging drop vapor diffusion method, using 2.0 M (NH4)2SO4, 0.1 M MES, pH 6.0, and 5% (v/v) isopropanol
crystal structure at 1.85 A resolution
-
crystal structure at 3 A resolution
-
crystal structure at 6.5 A resolution
-
hanging drop vapor diffusion method, packing of the octameric enzyme in the crystal form is unusual, because the asymmetric unit contains three subunits
-
muatnt enzyme F329I and I54V
X-ray crystal structure compared with that of mandelate racemase
-
sitting-drop vapor diffusion method
-
the crystallographic structure of the chloromuconate cycloisomerase from Rhodococcus opacus is determined at 2.5 A of resolution. Results highlight that a histidine, located in a loop that closes the active site cavity upon the binding of the substrate, could be related to the dehalogenation inability of Rho-2-CMCI
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.3
-
25°C, stable
3637
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
Frateuria sp.
-
10 min, 19% loss of activity of enzyme form MC II
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 24 h, complete loss of activity
-
-20°C, enzyme concentration 0.0035 mg/ml, 50 mM MOPS buffer, pH 6.5, 26% loss of activity after 2 months
-
-24°C, 3 weeks, 5% loss of activity
-
20°C, enzyme concentration 0.0035 mg/ml, 50 mM MOPS buffer, pH 6.5, 69% loss of activity after 2 months
-
4°C, 8 days, 6% loss of activity
-
4°C, enzyme concentration 0.0035 mg/ml, 50 mM MOPS buffer, pH 6.5, no loss of activity after 2 months
-
4°C, pH 7.0, enzyme retains more than 70% of the maximum activity after 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a single cycloisomerase with no isoforms
-
MonoQ column chromatography and Superose 12 gel filtration
native enzyme partially by anion exchange chromatography
-
nickel-affinity column chromatography and gel filtration
purified from cell extracts of salicylate-, 4-methylsalicylate-, or 5-chlorosalicylate-grown cells
Q-Sepharose column chromatography
-
recombinant enzyme
-
recombinant enzyme expressed in Escherichia coli JM105
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-RIL cells
expression in Escherichia coli or Pseudomonas putida
-
gene catB
-
part of gene cluster involved in degradation of substituted salicylates
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A271S
-
ratio of turnover number to Km-value: 1.5fold decrease with cis,cis-muconate as substrate, 3.3fold decrease with 2-chloro-cis,cis-muconate as substrate, 27fold increase with 3-chloro-cis,cis-muconate as substrate, 1.9fold decrease with 2,4-dichloro-cis,cis-muconate as substrate, 1.5fold decrease with 3-fluoro-cis,cis-muconate as substrate, 1.1fold increase with 2-methyl-cis,cis-muconate as substrate, 1.1fold decrease with 3-methyl-cis,cis-muconate as substrate
I54V/F329I
-
ratio of turnover number to Km-value: 81.5fold decrease with cis,cis-muconate as substrate, 2.6fold decrease with 2-chloro-cis,cis-muconate as substrate, 2.7fold increase with 3-chloro-cis,cis-muconate as substrate, 3.8fold increase with 2,4-dichloro-cis,cis-muconate as substrate, 2fold decrease with 3-fluoro-cis,cis-muconate as substrate, 4fold decrease with 2-methyl-cis,cis-muconate as substrate, 2fold decrease with 3-methyl-cis,cis-muconate as substrate
K169A
-
70000fold reduction in activity with cis,cis-muconate, 110000fold reduction in activity with 3-fluoro-cis,cis-muconate, 310fold reduction in activity with 3-chloro-cis,cis-muconate, 2.6fold reduction in activity with 2,4-dichloro-cis,cis-muconate. Wild-type enzyme forms protoanemonin and 2-chloroprotoanemonin from 3-chloro-cis,cis-muconate, mutant enzyme K169A forms cis-dienelactone and 2-chloro-cis-dienelactone
K276N
-
ratio of turnover number to Km-value: 10.7fold decrease with cis,cis-muconate as substrate, 8.7fold decrease with 2-chloro-cis,cis-muconate as substrate, 3.5fold increase with 3-chloro-cis,cis-muconate as substrate, 8.7fold decrease with 2,4-dichloro-cis,cis-muconate as substrate, 4.1fold decrease with 3-fluoro-cis,cis-muconate as substrate, 16.7fold decrease with 2-methyl-cis,cis-muconate as substrate, 12.1fold decrease with 3-methyl-cis,cis-muconate as substrate
L333V
-
ratio of turnover number to Km-value: 238fold decrease with cis,cis-muconate as substrate, 41.5fold decrease with 2-chloro-cis,cis-muconate as substrate, 3.4fold increase with 3-chloro-cis,cis-muconate as substrate, 5.9fold decrease with 2,4-dichloro-cis,cis-muconate as substrate, 1.4fold decrease with 3-fluoro-cis,cis-muconate as substrate, 34.6fold decrease with 2-methyl-cis,cis-muconate as substrate, 16.5fold decrease with 3-methyl-cis,cis-muconate as substrate
Y59W
-
ratio of turnover number to Km-value: 12.9fold decrease with cis,cis-muconate as substrate, nearly identical to wild-type value with 2-chloro-cis,cis-muconate as substrate, 4.4fold decrease with 3-fluoro-cis,cis-muconate, 1.8fold decrease with 2-methyl-cis,cis-muconate as substrate, 10.2fold decrease with 3-methyl-cis,cis-muconate as substrate
A271S
-
ratio of turnover number to Km-value: 1.5fold decrease with cis,cis-muconate as substrate, 3.3fold decrease with 2-chloro-cis,cis-muconate as substrate, 27fold increase with 3-chloro-cis,cis-muconate as substrate, 1.9fold decrease with 2,4-dichloro-cis,cis-muconate as substrate, 1.5fold decrease with 3-fluoro-cis,cis-muconate as substrate, 1.1fold increase with 2-methyl-cis,cis-muconate as substrate, 1.1fold decrease with 3-methyl-cis,cis-muconate as substrate
-
F329I
-
ratio of turnover number to Km-value: 5.7fold decrease with cis,cis-muconate as substrate, 1.6fold increase with 2-chloro-cis,cis-muconate as substrate, 3.4fold increase with 3-chloro-cis,cis-muconate as substrate, 3.2fold increase with 2,4-dichloro-cis,cis-muconate as substrate, 1.7fold decrease with 3-fluoro-cis,cis-muconate as substrate, 1.5fold increase with 2-methyl-cis,cis-muconate as substrate, 5.8fold decrease with 3-methyl-cis,cis-muconate as substrate
-
I54V
-
ratio of turnover number to Km-value: 11.9fold decrease with cis,cis-muconate as substrate, nearly identical to wild-type value with 2-chloro-cis,cis-muconate and 3-methyl-cis,cis-muconate as substrate, 22fold increase with 3-chloro-cis,cis-muconate as substrate, 1.67fold decrease with 2,4-dichloro-cis,cis-muconate as substrate, 5.8fold decrease with 3-fluoro-cis,cis-muconate as substrate, 8.8fold decrease with 2-methyl-cis,cis-muconate as substrate
-
K276N
-
ratio of turnover number to Km-value: 10.7fold decrease with cis,cis-muconate as substrate, 8.7fold decrease with 2-chloro-cis,cis-muconate as substrate, 3.5fold increase with 3-chloro-cis,cis-muconate as substrate, 8.7fold decrease with 2,4-dichloro-cis,cis-muconate as substrate, 4.1fold decrease with 3-fluoro-cis,cis-muconate as substrate, 16.7fold decrease with 2-methyl-cis,cis-muconate as substrate, 12.1fold decrease with 3-methyl-cis,cis-muconate as substrate
-
Y59W
-
ratio of turnover number to Km-value: 12.9fold decrease with cis,cis-muconate as substrate, nearly identical to wild-type value with 2-chloro-cis,cis-muconate as substrate, 4.4fold decrease with 3-fluoro-cis,cis-muconate, 1.8fold decrease with 2-methyl-cis,cis-muconate as substrate, 10.2fold decrease with 3-methyl-cis,cis-muconate as substrate
-
T52G
-
turnover number with cis,cis-muconate is 52.5fold lower than that of the wild-type enzyme, Km-value for cis,cis-muconate is 3.9fold higher than that of wild-type enzyme
T52G/F103S
-
turnover number with cis,cis-muconate is 12fold lower than that of the wild-type enzyme, Km-value for cis,cis-muconate is 3.6fold higher than that of wild-type enzyme
Show AA Sequence (574 entries)
Please use the Sequence Search for a specific query.