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Information on EC 5.5.1.5 - Carboxy-cis,cis-muconate cyclase
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5.5.1.5 Carboxy-cis,cis-muconate cyclaseSpecify your search results
Word Map
- 5.5.1.5
-
humoral
-
lactonizing
-
neurospora
- niger
- brasiliensis
- aspergillus
- schenckii
- sporothrix
- sporotrichosis
- 3-carboxy-cis,cis-muconate
-
cycloisomerase
-
regiochemical
-
5.5.1.1
-
stereochemical
- crassa
-
gamma-lactone
-
zoonotic
-
scratches
-
bites
-
warm-blooded
- globosa
-
eucaryotic
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
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-, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-Carboxy-cis,cis-muconate lactonizing enzyme
CMLE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate
syn-1,2 addition-elimination reaction
-
3-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 3-carboxy-cis,cis-muconate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
KEGG
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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
37318-55-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
enzyme of the protocatechuate catabolic pathway
-
-
?
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
coordinate induction of 3-carboxymuconate cyclase, 3-carboxymuconolactone hydrolase and 3-oxoadipate CoA-transferase by either protocatechuate or p-hydroxybenzoate
-
-
?
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
enzyme of the protocatechuate branch of the 3-oxoadipate pathway
-
-
?
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
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
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
3-carboxymuconolactone
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
r
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
3-Carboxy-cis,cis-muconate
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
enzyme of the protocatechuate catabolic pathway
-
-
?
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
coordinate induction of 3-carboxymuconate cyclase, 3-carboxymuconolactone hydrolase and 3-oxoadipate CoA-transferase by either protocatechuate or p-hydroxybenzoate
-
-
?
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
enzyme of the protocatechuate branch of the 3-oxoadipate pathway
-
-
?
3-Carboxy-5-oxo-2,5-dihydrofuran-2-acetate
?
-
3-carboxymuconate cyclase and 3-carboxymuconolactone hydrolase are under coordinate control
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-carboxy-cis,cis-muconate
-
substrate inhibition at concentration exceeding 0.070 mM
BO33-
-
negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum
ethoxyformic anhydride
-
irreversible, presence of the competitive inhibitors cis-aconitate, trans-aconitate and cis,cis-muconate conferrs some protection
H2PO2-
-
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
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Sporotrichosis
Proteomics-Based Characterization of the Humoral Immune Response in Sporotrichosis: Toward Discovery of Potential Diagnostic and Vaccine Antigens.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CMLE_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
366
0
41329
Swiss-Prot
other Location (Reliability: 4)
B8MT79_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
371
0
41820
TrEMBL
Mitochondrion (Reliability: 5)
J9VY29_LACBU
347
0
38388
TrEMBL
-
A0A084FZ43_PSEDA
1219
0
135390
TrEMBL
other Location (Reliability: 5)
A0A1W2TJF4_ROSNE
361
0
40343
TrEMBL
other Location (Reliability: 5)
A2QAI9_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
368
0
41311
TrEMBL
other Location (Reliability: 5)
A0A0T8U4Q0_9STRE
337
0
37672
TrEMBL
-
Q1GB62_LACDA
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778)
336
0
37298
TrEMBL
-
H9C592_FUSOX
364
0
41106
TrEMBL
Secretory Pathway (Reliability: 5)
U3PRP6_9PEZI
412
0
43180
TrEMBL
Secretory Pathway (Reliability: 2)
A0A068VU86_PROFF
349
0
38268
TrEMBL
-
U3PUQ3_SPOSC
413
0
43379
TrEMBL
Secretory Pathway (Reliability: 1)
D7GHV2_PROFC
Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1)
349
0
38268
TrEMBL
-
D2BNA9_LACLK
Lactococcus lactis subsp. lactis (strain KF147)
341
0
37302
TrEMBL
-
G0AID8_COLFT
Collimonas fungivorans (strain Ter331)
410
0
44461
TrEMBL
-
A0A0T8TLP8_9STRE
337
0
37667
TrEMBL
-
A0A0A8R5G0_9ACTN
349
0
38268
TrEMBL
-
A0A0F8BK18_CERFI
1161
0
129760
TrEMBL
Secretory Pathway (Reliability: 5)
G0L8P3_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
383
0
41605
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
-
8 * 24000, equilibrium sedimentation in presence of 5 M guanidine hydrochloride and 2-mercaptoethanol, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
-
8 * 24000, equilibrium sedimentation in presence of 5 M guanidine hydrochloride and 2-mercaptoethanol, SDS-PAGE
tetramer
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thatcher, D.R.; Cain, R.B.
Metabolism of aromatic compounds by fungi. 1. Purification and physical properties of 3-carboxy-cis-cis-muconate cyclase from Aspergillus niger
Eur. J. Biochem.
48
549-556
1974
Aspergillus niger
brenda
Thatcher, D.R.; Cain, R.B.
Metabolism of aromatic compounds by fungi. 2. Subunit structure of the 3-carboxy-cis-cis-muconate cyclase of Aspergillus niger
Eur. J. Biochem.
48
557-562
1974
Aspergillus niger
brenda
Cook, K.A.; Cain, R.B.
Regulation of aromatic metabolism in the fungi: metabolic control of the 3-oxoadipate pathway in the yeast Rhodotorula mucilaginosa
J. Gen. Microbiol.
85
37-50
1974
Rhodotorula mucilaginosa
brenda
Huber, T.J.; Street, J.R.; Bull, A.T.; Cook, K.A.; Cain, R.B.
Aromatic metabolism in the fungi. Growth of Rhodotorula mucilaginosa, in p-hydroxybenzoate-limited chemostats and the effect of growth rate on the synthesis of enzymes of the 3-oxoadipate pathway
Arch. Microbiol.
102
139-144
1975
Rhodotorula mucilaginosa
brenda
Thatcher, D.R.; Cain, R.B.
Metabolism of aromatic compounds by fungi. Kinetic properties and mechanism of 3-carboxy-cis,cis-muconate cyclase from Aspergillus niger
Eur. J. Biochem.
56
193-204
1975
Aspergillus niger
brenda
Cook, K.A.; Cain R.B.
Enzymes of the 3-oxoadipate pathway in fungi: a serological study of 3-carboxymuconate cyclase (lactonizing enzyme) in fungi and its possible taxonomic significance
J. Gen. Microbiol.
102
81-94
1977
Aspergillus amstelodami, Aspergillus fischeri, Aspergillus flavus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Aspergillus sydowii, Aspergillus terreus, Amorphotheca resinae, Trichoderma deliquescens, Clonostachys rosea, Kernia nitida, Monascus ruber, Byssochlamys spectabilis, Penicilliopsis clavariiformis, Penicillium capsulatum, Penicillium commune, Penicillium terrestre
-
brenda
Mazur, P.; Henzel, W.J.; Mattoo, S.; Kozarich, J.W.
3-Carboxy-cis-cis-muconate lactonizing enzyme from Neurospora crassa: an alternate cycloisomerase motif
J. Bacteriol.
176
1718-1728
1994
Aspergillus niger, Neurospora crassa
brenda
Michielse, C.B.; Reijnen, L.; Olivain, C.; Alabouvette, C.; Rep, M.
Degradation of aromatic compounds through the alpha-ketoadipate pathway is required for pathogenicity of the tomato wilt pathogen Fusarium oxysporum f. sp. lycopersici
Mol. Plant Pathol.
13
1089-1100
2012
Fusarium oxysporum
brenda
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