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Information on EC 4.1.1.44 - 4-carboxymuconolactone decarboxylase
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EC Tree
4.1.1.44 4-carboxymuconolactone decarboxylaseSpecify your search results
Word Map
- 4.1.1.44
-
beta-ketoadipate
- putida
- protocatechuate
- beta-carboxy-cis,cis-muconate
- acinetobacter
- decarboxylases
-
lactonizing
- calcoaceticus
-
hexamers
- phthalate
-
succinyl-coenzyme
-
cycloisomerase
- rhizobium
- rhodococcus
- leguminosarum
- trifolii
- tumefaciens
-
3,4-dioxygenase
-
isofunctional
-
taxon
-
nonidentical
- japonicum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
gamma-carboxymuconolactone decarboxylase, 4-carboxymuconolactone decarboxylase, gamma-cmd, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase
CMD
-
-
-
-
gamma-carboxymuconolactone decarboxylase
PcaC
PcaL
3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase
EC 3.1.1.24 and EC 4.1.1.44, respectively
3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase
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bifunctional enzyme
3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase
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bifunctional enzyme
-
gamma-carboxymuconolactone decarboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 4,5-dihydro-5-oxofuran-2-acetate + CO2
syn-reaction
-
(R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = 4,5-dihydro-5-oxofuran-2-acetate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-carboxy-2,5-dihydro-5-oxofuran-2-acetate carboxy-lyase (4,5-dihydro-5-oxofuran-2-acetate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
37289-46-6
-
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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
additional information
?
-
enzyme additionally catalyzes the conversion of product beta-oxoadipate enol-lactone to beta-oxoadipate, reaction of EC 3.1.1.24
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
beta-ketoadipate enol-lactone
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
(4R,5R)-5-[2H]-4-carboxymuconolactone
(2R,5R)-2,5-di[2H]enol-lactone
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran-2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
?
-
enzyme of the beta-ketoadipate pathway
-
-
?
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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
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
-
?
4-carboxymuconolactone
5-oxo-4,5-dihydrofuran 2-acetate + CO2
-
-
-
?
4-carboxymuconolactone
?
-
enzyme of the beta-ketoadipate pathway
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional 3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase, EC 3.1.1.24 and EC 4.1.1.44, respectively
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
spatially associated with the basal body, a part of the cytoskeletal organizing center
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
CMD1 accumulated upon treatment with the G2/M inhibitor nocodazole. CMD1 is expressed and transported to/from the basal body during cytokinesis, suggesting a role in cell division
Show AA Sequence and Transmembrane Helices (4247 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13300
85500
additional information
additional information
-
homologies in the NH2-terminal amino acid sequences of gamma-carboxymuconolactone decarboxylases and muconolactone isomerases, ec 5.3.3.4
additional information
-
homologies in the NH2-terminal amino acid sequences of gamma-carboxymuconolactone decarboxylases and muconolactone isomerases, ec 5.3.3.4
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, 22%(w/v) polyethylene glycol 3350, 0.2 M sodium chloride, 0.1 M Na HEPES pH 7.0 and 10%(v/v) glycerol, the crystal belongs to space group P43212, with unit-cell parameters a = b = 66.66, c = 184.82 A, resolution 2.40 A, the Matthews coefficient and solvent content are estimated to be 2.14 A3/Da and 42.6%, respectively, assuming that the asymmetric unit contains three recombinant protein molecules
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of 3-oxoadipate enol-lactone-hydrolyzing activity, ec 3.1.1.24 and 4-carboxymuconolactone-decarboxylating activity, ec 4.1.1.44
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ornston, L.N.
Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)
Methods Enzymol.
17A
529-549
1970
Pseudomonas putida
-
brenda
Chari, R.V.J.; Whitman, C.P.; Kozarich, J.W.; Ngai, K.L.; Ornston, L.N.
Absolute stereochemical course of muconolactone DELTA-isomerase and of 4-carboxymuconolactone decarboxylase: A 1H NMR "Ricochet" analysis
J. Am. Chem. Soc.
109
5520-5521
1987
Acinetobacter calcoaceticus, Pseudomonas putida
-
brenda
Parke, D.; Ornston, L.N.
Enzymes of the beta-ketoadipate pathway are inducible in Rhizobium and Agrobacterium spp. and constitutive in Bradyrhizobium spp.
J. Bacteriol.
165
288-292
1986
Agrobacterium tumefaciens, Agrobacterium rhizogenes, Bradyrhizobium japonicum, Bradyrhizobium sp., Sinorhizobium fredii, Rhizobium leguminosarum, Sinorhizobium meliloti
brenda
Doten, R.C.; Ngai, K.L.; Mitchell, D.J.; Ornston, L.N.
Cloning and genetic organization of the pca gene cluster from Acinetobacter calcoaceticus
J. Bacteriol.
169
3168-3174
1987
Acinetobacter calcoaceticus
brenda
Eulberg, D.; Lakner, S.; Golovleva, L.A.; Schlmann, M.
Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity
J. Bacteriol.
180
1072-1081
1998
Rhodococcus opacus, Rhodococcus opacus 1CP
brenda
Yeh, W.K.; Durham, D.R.; Fletcher, P.; Ornston, L.N.
Evolutionary relationships among gamma-carboxymuconolactone decarboxylases
J. Bacteriol.
146
233-238
1981
Azotobacter vinelandii, Acinetobacter calcoaceticus, Pseudomonas putida
brenda
Yeh, W.K.; Fletcher, P.; Ornston, N.
Homologies in the NH2-terminal amino acid sequences of gamma-carboxymuconolactone decarboxylases and muconolactone isomerases
J. Biol. Chem.
255
6347-6354
1980
Acinetobacter calcoaceticus, Pseudomonas putida
brenda
Parke, D.; Meagher, R.B.; Ornston, L.N.
Relationships among enzymes of the beta-ketoadipate pathway. 3. Properties of crystalline gamma-carboxymuconolactone decarboxylase from Pseudomonas putida
Biochemistry
12
3537-3542
1973
Pseudomonas putida
brenda
Hara, H.; Eltis, L.D.; Davies, J.E.; Mohn, W.W.
Transcriptomic analysis reveals a bifurcated terephthalate degradation pathway in Rhodococcus sp. strain RHA1
J. Bacteriol.
189
1641-1647
2007
Rhodococcus sp., Rhodococcus sp. RHA1
brenda
Buchan, A.; Neidle, E.L.; Moran, M.A.
Diverse organization of genes of the beta-ketoadipate pathway in members of the marine Roseobacter lineage
Appl. Environ. Microbiol.
70
1658-1668
2004
Sulfitobacter pontiacus, Sulfitobacter sp. (Q6SJA7), Ruegeria pomeroyi (Q6SJB9), Roseovarius nubinhibens ISM (Q6SJC5), Sagittula stellata E-37 (Q9L5B1), Sulfitobacter pontiacus ChLG 10
brenda
Lee, H.Y.; Yang, J.K.
Crystallization and preliminary X-ray crystallographic analysis of gamma-carboxymucolactone decarboxylase from Sulfolobus solfataricus
Acta Crystallogr. Sect. F
65
1197-1199
2009
Saccharolobus solfataricus
brenda
Yamanashi, T.; Kim, S.Y.; Hara, H.; Funa, N.
In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL the protocatechuate branch of the beta-ketoadipate pathway in Rhodococcus jostii RHA1
Biosci. Biotechnol. Biochem.
79
830-835
2015
Rhodococcus jostii (Q0SH24)
brenda
Cheng, W.; Huang, K.; Huang, P.; Lee, C.; Yeh, Y.; Ku, F.; Lin, R.; Cheng, M.; Chiu, C.; Tang, P.
gamma-Carboxymuconolactone decarboxylase A novel cell cycle-related basal body protein in the early branching eukaryote Trichomonas vaginalis
Parasit. Vectors
10
443
2017
Trichomonas vaginalis (A2FEX8)
brenda
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