Information on EC 5.5.1.5 - Carboxy-cis,cis-muconate cyclase

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The expected taxonomic range for this enzyme is: Dikarya

EC NUMBER
COMMENTARY
5.5.1.5
-
RECOMMENDED NAME
GeneOntology No.
Carboxy-cis,cis-muconate cyclase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate
show the reaction diagram
syn-1,2 addition-elimination reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination/addition
-
-
intramolecular
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3-carboxy-5-oxo-2,5-dihydrofuran-2-acetate (decyclizing)
-
-
-
-
3-Carboxy-cis,cis-muconate lactonizing enzyme
-
-
-
-
3-Carboxy-cis,cis-muconate lactonizing enzyme
-
-
3-Carboxy-cis-cis-muconate cyclase
-
-
-
-
3-Carboxymuconate cyclase
-
-
-
-
CMLE
-
-
-
-
Cyclase, carboxy-cis,cis-muconate-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37318-55-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
deletion mutant cannot catabolize phenolic compounds known to be degraded via the beta-ketoadipate pathway. Mutant is impaired in root invasion and is nonpathogenic, even though it shows normal superficial root colonization
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
-
coordinate induction of 3-carboxymuconate cyclase, 3-carboxymuconolactone hydrolase and 3-oxoadipate CoA-transferase by either protocatechuate or p-hydroxybenzoate, enzyme of the protocatechuate branch of the 3-oxoadipate pathway
-
-
-
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
-
enzyme of the protocatechuate catabolic pathway
-
-
-
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
-
3-carboxymuconate cyclase and 3-carboxymuconolactone hydrolase are under coordinate control
-
-
-
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
-
-
-
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
-
-
-
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
-
-
-
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
-
-
-
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
3-carboxymuconolactone
-
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
r
-
-
-
cis,cis-Muconate
5-Oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
-
coordinate induction of 3-carboxymuconate cyclase, 3-carboxymuconolactone hydrolase and 3-oxoadipate CoA-transferase by either protocatechuate or p-hydroxybenzoate, enzyme of the protocatechuate branch of the 3-oxoadipate pathway
-
-
-
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
-
enzyme of the protocatechuate catabolic pathway
-
-
-
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
-
3-carboxymuconate cyclase and 3-carboxymuconolactone hydrolase are under coordinate control
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
contains 0.06 M to 0.3 M of Ca2+ per mol of subunit
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Chloro-4-methylmuconolactone
-
non-competitive
3-carboxy-cis,cis-muconate
-
substrate inhibition at concentration exceeding 0.070 mM
3-chloromuconate
-
competitive
3-Chloromuconolactone
-
non-competitive
3-methylmuconate
-
competitive
Adipate
-
-
AsO43-
-
-
BO33-
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
cis-aconitate
-
-
citraconate
-
-
citrate
-
-
Ethoxyformic anhydride
-
irreversible, presence of the competitive inhibitors cis-aconitate, trans-aconitate and cis,cis-muconate conferrs some protection
fumarate
-
-
glutaconate
-
-
Glutarate
-
-
Itaconate
-
-
malate
-
-
Maleate
-
-
malonate
-
-
mesaconate
-
-
Na2H2PO2
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
-
oxalate
-
-
phosphate
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
pimelate
-
-
S2O32-
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
succinate
-
-
Tartrate
-
-
trans,trans-muconate
-
-
trans-aconitate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0103
3-carboxy-cis,cis-muconate
-
recombinant enzyme expressed in E. coli
0.0207
3-carboxy-cis,cis-muconate
-
-
0.057
3-carboxy-cis,cis-muconate
-
-
26.2
cis,cis-Muconate
-
recombinant enzyme expressed in E. coli
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
360
3-carboxy-cis,cis-muconate
-
-
382
3-carboxy-cis,cis-muconate
-
recombinant enzyme expressed in E. coli
1.1
cis,cis-Muconate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
600
-
recombinant enzyme expressed in Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6
-
-
7
-
broad around
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
158000
-
gel filtration
3720
191000
-
high-speed equilibrium sedimentation
3714
200000
-
gel filtration
3714
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
-
8 * 24000, equilibrium sedimentation in presence of 5 M guanidine hydrochloride and 2-mercaptoethanol, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE, 4 * 41200, calculation from nucleotide sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
hexose composition of 9.54% which can be equivalent to 14.2 residues per polypeptide chain of MW 24000. An N-acetylglucosamine concentration of 2.8% is determined which can be equivalent to 3.9 residues per polypeptide chain
no glycoprotein
-
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rose-bengal-sensitized photooxidation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for over 9 months in the intact mycelium
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-