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Information on EC 4.1.1.46 - o-pyrocatechuate decarboxylase
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4.1.1.46 o-pyrocatechuate decarboxylaseSpecify your search results
Word Map
- 4.1.1.46
- decarboxylases
- aspergillus
-
non-oxidative
- niger
- oxysporum
-
fusarium
-
biocatalytic
-
biocatalysts
- n-ethylmaleimide
- rhizobium
- indole
- oryzae
-
metal-dependent
- synthesis
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homotetrameric
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
2,3-DHBA decarboxylase, 2,3-Dihydroxybenzoic acid decarboxylase, Decarboxylase, o-pyrocatechuate, DHBA decarboxylase, DHBD, FOIG_04675, o-Pyrocatechuic acid carboxy-lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-DHBA decarboxylase
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-
-
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2,3-Dihydroxybenzoic acid decarboxylase
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-
-
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Decarboxylase, o-pyrocatechuate
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-
-
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DHBA decarboxylase
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-
-
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DHBD
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-
-
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o-Pyrocatechuic acid carboxy-lyase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-dihydroxybenzoate = catechol + CO2
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2,3-dihydroxybenzoate carboxy-lyase (catechol-forming)
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CAS REGISTRY NUMBER
COMMENTARY
37289-48-8
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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
2,3,5-Trihydroxybenzoate
1,2,4-Trihydroxybenzene + CO2
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18% of the activity with 2,3-dihydroxybenzoate
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-
?
3-fluoro-2-hydroxybenzoate
2-fluorophenol + CO2
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-
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r
3-methoxy-6-hydroxybenzoate
3-methoxyphenol + CO2
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-
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r
3-methoxyphenol + CO2
3-methoxy-6-hydroxybenzoate
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-
-
?
2,3-Dihydroxybenzoate
?
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enzyme is involved in the pathway for the biodegradation of indole, enzyme is induced by indole
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-
?
2,3-Dihydroxybenzoate
?
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enzyme is involved in the biosynthesis of catechol
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-
?
2,3-Dihydroxybenzoate
?
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enzyme is involved in the catabolism of Trp, induced by both L-Trp and salicylate
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-
?
2,3-Dihydroxybenzoate
?
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induced to over 6times its basal level by the addition of 0.1% Trp
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-
?
additional information
?
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enzyme catalyzes the decarboxylation of various substituted salicylic acids with different groups at varied positions except 5-position and the carboxylation of phenol and the substituted phenols
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-
?
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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
2,3-Dihydroxybenzoate
?
-
enzyme is involved in the pathway for the biodegradation of indole, enzyme is induced by indole
-
-
?
2,3-Dihydroxybenzoate
?
-
enzyme is involved in the biosynthesis of catechol
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-
?
2,3-Dihydroxybenzoate
?
-
enzyme is involved in the catabolism of Trp, induced by both L-Trp and salicylate
-
-
?
2,3-Dihydroxybenzoate
?
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induced to over 6times its basal level by the addition of 0.1% Trp
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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kcat/KM VALUE [1/mMs-1]
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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
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pH 4.5: about 35% of maximal activity, pH 7.0: about 30% of maximal activity
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TEMPERATURE 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
-
with increasing mycelial age, the basal enzyme activity level remains relatively unchanged, while the level to which the enzyme could be induced decreases significantly
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
?
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x * 38000, SDS-PAGE, x * 38400, calculated from sequence, recombinant protein with His-tag
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
2 h, 45% residual decarboxylase activity, 40% residual carboxylase activity
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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
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
construction of an artificial pathway for muconic acid production in Escherichia coli by connecting 2,3-dihydroxybenzoic acid biosynthesis with its degradation pathway. Overexpression of entCBA and the key enzymes in the shikimate pathway leads to the production of 900 mg/l of 2,3-dihydroxybenzoic acid. Expression of 2,3-dihydroxybenzoic acid decarboxylase coupled with catechol 1,2-dioxygenase achieves the conversion of 2,3-dihydroxybenzoic acid into muconic acid. Assembly of the total pathway results in the de novo production of muconic acid up to 480 mg/l
synthesis
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development of an artificial pathway in Escherichia coli for the biosynthesis of muconic acid. Expression of 2,3-dihydroxybenzoate decarboxylase and catechol 1,2-dioxygenase and metabolic optimization by increasing the flux from chorismate through the enterobactin biosynthesis pathway and by regulating the shikimate pathway leads to synthesis of 605.18 mg/l of muconic acid from glucose in a shaking flask culture
synthesis
Klebsiella pneumoniae CICIM B7001
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development of an artificial pathway in Escherichia coli for the biosynthesis of muconic acid. Expression of 2,3-dihydroxybenzoate decarboxylase and catechol 1,2-dioxygenase and metabolic optimization by increasing the flux from chorismate through the enterobactin biosynthesis pathway and by regulating the shikimate pathway leads to synthesis of 605.18 mg/l of muconic acid from glucose in a shaking flask culture
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kamath, A.V.; Dasgupta, D.; Vaidyanathan, C.S.
Enzyme-catalysed non-oxidative decarboxylation of aromatic acids. I. Piurification and spectroscopic properties of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus niger
Biochem. Biophys. Res. Commun.
145
586-595
1987
Aspergillus niger
brenda
Anderson, J.J.; Dagley, S.
Catabolism of tryptophan, anthranilate, and 2,3-dihydroxybenzoate in Trichosporon cutaneum
J. Bacteriol.
146
291-297
1981
Cutaneotrichosporon cutaneum
brenda
Ramachandran, A.; Subramanian, V.; Sugumaran, M.; Vaidyanathan, C.S.
Purification and properties of pyrocatechuate decarboxylase from Aspergillus niger
FEMS Microbiol. Lett.
5
421-425
1979
Aspergillus nidulans, Aspergillus niger, Colletotrichum gloeosporioides, Trichoderma viride, Aspergillus niger UBC814
-
brenda
Subba Rao, P.V.; Moore, K.; Towers, G.H.N.
o-Pyrocatechuic acid carboxy-lyase (Aspergillus niger)
Methods Enzymol.
17A
514-518
1970
Aspergillus niger
-
brenda
Subba Rao, P.V.; Moore, K.; Towers, G.H.N.
o-Pyrocatechuic acid carboxy-lyase from Aspergillus niger
Arch. Biochem. Biophys.
122
466-473
1967
Aspergillus niger
brenda
Spiegelman, B.M.; Coursen, B.W.
Age-related changes associated with the induction of o-pyrocatechuic acid carboxylase in Aspergillus ornatus
Arch. Microbiol.
104
33-37
1975
Sclerocleista ornata
brenda
Santha, R.; Rao, N.A.; Vaidyanathan, C.S.
Identification of the active-site peptide of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus oryzae
Biochim. Biophys. Acta
1293
191-200
1996
Aspergillus oryzae
brenda
Kamath, A.V.; Rao, N.A.; Vaidyanathan, C.S.
Enzyme catalysed non-oxidative decarboxylation of aromatic acids. II. Identification of active site residues of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus niger
Biochem. Biophys. Res. Commun.
165
20-26
1989
Aspergillus niger
brenda
Santha, R.; Savithri, H.S.; Rao, N.A.; Vaidyanathan, C.S.
2,3-Dihydroxybenzoic acid decarboxylase from Aspergillus niger. A novel decarboxylase
Eur. J. Biochem.
230
104-110
1995
Aspergillus niger
brenda
Kamath, A.V.; Vaidyanathan, C.S.
New pathway for the biodegradation of indole in Aspergillus niger
Appl. Environ. Microbiol.
56
275-280
1990
Aspergillus niger
brenda
Sun, X.; Lin, Y.; Yuan, Q.; Yan, Y.
Biological production of muconic acid via a prokaryotic 2,3-dihydroxybenzoic acid decarboxylase
ChemSusChem
7
2478-2481
2014
Klebsiella pneumoniae
brenda
Zhang, X.; Ren, J.; Yao, P.; Gong, R.; Wang, M.; Wu, Q.; Zhu, D.
Biochemical characterization and substrate profiling of a reversible 2,3-dihydroxybenzoic acid decarboxylase for biocatalytic Kolbe-Schmitt reaction
Enzyme Microb. Technol.
113
37-43
2018
Fusarium odoratissimum NRRL 54006 (X0JT48)
brenda
Wang, J.; Zheng, P.
Muconic acid production from glucose using enterobactin precursors in Escherichia coli
J. Ind. Microbiol. Biotechnol.
42
701-709
2015
Klebsiella pneumoniae, Klebsiella pneumoniae CICIM B7001
brenda
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