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 ACCESSION NO.
LITERATURE
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate
show the reaction diagram
-
-
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
elimination/addition
-
-
intramolecular
-
PATHWAY
KEGG Link
MetaCyc Link
Benzoate degradation
-
SYSTEMATIC NAME
IUBMB Comments
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-carboxy-5-oxo-2,5-dihydrofuran-2-acetate (decyclizing)
-
-
-
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
contains 0.06 M to 0.3 M of Ca2+ per mol of subunit
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
BO33-
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
cis-aconitate
-
-
citraconate
-
-
Ethoxyformic anhydride
-
irreversible, presence of the competitive inhibitors cis-aconitate, trans-aconitate and cis,cis-muconate conferrs some protection
glutaconate
-
-
Maleate
-
-
-
Na2H2PO2
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
-
phosphate
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
S2O32-
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
trans,trans-muconate
-
-
trans-aconitate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
600
-
-
recombinant enzyme expressed in Escherichia coli
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
broad around
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
158000
-
-
gel filtration
191000
-
-
high-speed equilibrium sedimentation
200000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
LITERATURE
rose-bengal-sensitized photooxidation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable for over 9 months in the intact mycelium
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-