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

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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
5.5.1.5
-
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RECOMMENDED NAME
GeneOntology No.
Carboxy-cis,cis-muconate cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination/addition
-
-
intramolecular
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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-
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SYSTEMATIC NAME
IUBMB Comments
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-55-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
var. glaber
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
cis,cis-Muconate
5-Oxo-2,5-dihydrofuran-2-acetate
show the reaction diagram
-
-
-
-
-
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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-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
contains 0.06 M to 0.3 M of Ca2+ per mol of subunit
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Chloro-4-methylmuconolactone
-
non-competitive
3-carboxy-cis,cis-muconate
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substrate inhibition at concentration exceeding 0.070 mM
3-chloromuconate
-
competitive
3-Chloromuconolactone
-
non-competitive
3-methylmuconate
-
competitive
adipate
-
-
AsO43-
-
-
BO33-
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negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
cis-aconitate
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citraconate
-
-
citrate
-
-
Ethoxyformic anhydride
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irreversible, presence of the competitive inhibitors cis-aconitate, trans-aconitate and cis,cis-muconate conferrs some protection
fumarate
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glutaconate
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Glutarate
-
-
Itaconate
-
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malate
-
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Maleate
-
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malonate
-
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mesaconate
-
-
Na2H2PO2
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negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
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oxalate
-
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phosphate
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negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
pimelate
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S2O32-
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negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
succinate
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Tartrate
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trans,trans-muconate
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trans-aconitate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0103 - 0.057
3-carboxy-cis,cis-muconate
26.2
cis,cis-muconate
-
recombinant enzyme expressed in E. coli
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
360 - 382
3-carboxy-cis,cis-muconate
1.1
cis,cis-muconate
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
600
-
recombinant enzyme expressed in Escherichia coli
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
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-
7
-
broad around
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
8 * 24000, equilibrium sedimentation in presence of 5 M guanidine hydrochloride and 2-mercaptoethanol, SDS-PAGE
41000
-
4 * 41000, SDS-PAGE
41200
-
4 * 41200, calculation from nucleotide sequence
158000
-
gel filtration
191000
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high-speed equilibrium sedimentation
200000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
-
8 * 24000, equilibrium sedimentation in presence of 5 M guanidine hydrochloride and 2-mercaptoethanol, SDS-PAGE
tetramer
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4 * 41000, SDS-PAGE; 4 * 41200, calculation from nucleotide sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rose-bengal-sensitized photooxidation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for over 9 months in the intact mycelium
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 5.5.1.5)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)