Information on EC 5.5.1.1 - Muconate cycloisomerase

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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
Benzoate degradation
-
-
catechol degradation to beta-ketoadipate
-
-
Chlorocyclohexane and chlorobenzene degradation
-
-
Fluorobenzoate degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Toluene degradation
-
-
phenol degradation
-
-
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
strain R3
-
-
Manually annotated by BRENDA team
strain R3
-
-
Manually annotated by BRENDA team
strain BA-5-17
-
-
Manually annotated by BRENDA team
strain BA-5-17
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
335; basonym Alcaligenes eutrophus; JMP134
-
-
Manually annotated by BRENDA team
335
-
-
Manually annotated by BRENDA team
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
strain RW41
-
-
Manually annotated by BRENDA team
strain RW41
-
-
Manually annotated by BRENDA team
GJ31
-
-
Manually annotated by BRENDA team
WR1323
-
-
Manually annotated by BRENDA team
strain MT1, isoform SalC
SwissProt
Manually annotated by BRENDA team
B1
-
-
Manually annotated by BRENDA team
B13
-
-
Manually annotated by BRENDA team
strain MT1, isoform catB
-
-
Manually annotated by BRENDA team
RHO1
-
-
Manually annotated by BRENDA team
strain 1G
-
-
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
Pseudomonas reinekei
C6YXG6
-
8.8 - 57600
3-chloro-cis,cis-muconate
111
3-chloromuconate
Pseudomonas reinekei
C6YXG6
-
156000 - 534000
3-fluoro-cis,cis-muconate
2 - 108000
3-methyl-cis,cis-muconate
11
3-methylmuconate
Pseudomonas reinekei
C6YXG6
-
4 - 756000
cis,cis-muconate
1.4
muconolactone
Pseudomonas putida
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
2-methylmuconate
Pseudomonas reinekei
C6YXG6
-
21774
1100
3-chloromuconate
Pseudomonas reinekei
C6YXG6
-
16033
1000
3-methylmuconate
Pseudomonas reinekei
C6YXG6
-
20615
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 - 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
6 - 7
-
less than 50% of maximal activity below pH 6 and above pH 7
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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Rhizobium meliloti (strain 1021)
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
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 (532 entries)
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