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Enzyme Nomenclature
Information on EC 4.1.1.91 - salicylate decarboxylase
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The expected taxonomic range for this enzyme is: Cutaneotrichosporon moniliiforme
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EC NUMBER 
COMMENTARY 
4.1.1.91
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RECOMMENDED NAME
GeneOntology No.
salicylate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
salicylate = phenol + CO2
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
salicylate carboxy-lyase
In the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylate. The enzyme also catalyses the reversible decarboxylation of 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2,3-dihydroxybenzoate and 4-aminosalicylate [1].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
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i.e gamma-resorcylic acid
i.e. resorcinol
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r
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
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i.e. catechol
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r
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
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i.e. catechol
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r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
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i.e beta-resorcylic acid
i.e. resorcinol
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r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
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i.e beta-resorcylic acid
i.e. resorcinol
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r
salicylate
phenol + CO2
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in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid
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r
salicylate
phenol + CO2
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in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid
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r
additional information
?
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the enzyme does not catalyse the carboxylation of cresol. The enzyme does not catalyse the decarboxylation of 3-hydroxybenzoate, 4-hydroxybenzoate, 3,4-dihydroxybenzoate, 5-dihydroxybenzoate, 3-methylsalicylate, 4-methylsalicylate, and vanillic acid (4-hydroxy-3-methoxybenzoate). The substrate recognition of the enzyme for decarboxylation seems to depend strictly on hydroxybenzoic acid with two neighboring hydroxyl and carboxyl groups in the active center of the enzyme
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additional information
?
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the enzyme does not catalyse the carboxylation of cresol. The enzyme does not catalyse the decarboxylation of 3-hydroxybenzoate, 4-hydroxybenzoate, 3,4-dihydroxybenzoate, 5-dihydroxybenzoate, 3-methylsalicylate, 4-methylsalicylate, and vanillic acid (4-hydroxy-3-methoxybenzoate). The substrate recognition of the enzyme for decarboxylation seems to depend strictly on hydroxybenzoic acid with two neighboring hydroxyl and carboxyl groups in the active center of the enzyme
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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the enzyme does not require pyridoxal 5'-phosphate, NADH, and NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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1 mM, 1.5fold stimulation of carboxylation activity, no effect on decarboxylation activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AgNO3
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1 mM, complete loss of decarboxylation activity, 60% loss of carboxylation activity
CuCl2
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1 mM, 70% loss of carboxylation activity, 14% loss of decarboxylation activity
diethyl dicarbonate
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1 mM, 37% inhibition of carboxylation activity, 21% inhibition of decarboxylation activity
HgCl2
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1 mM, complete inhibition of decarboxylation activity, 94% loss of carboxylation activity
hydroxylamine
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1 mM, 23% inhibition of carboxylation activity, 9% inhibition of decarboxylation activity
NEM
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1 mM, 28% loss of carboxylation activity, 6% loss of decarboxylation activity
NiCl2
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1 mM, 85% loss carboxylation activity, 46% loss of decarboxylation activity
p-chloromercuribenzoic acid
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0.2 mM, 49% loss of carboxylation activity, 82% loss of decarboxylation activity
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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
0.47
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pH 5.5, 40°C, production of phenol from salicylic acid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
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pH 5.0: about 75% of maximal activity, pH 8.5: about 50% of maximal activity, production of phenol from salicylate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
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20°C: about 35% of maximal activity, 30°C: maximal activity, 40°C: about 10% of maximal activity, production of salicylate from phenol
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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1 h, decarboxylation activity is stable up to, 60% of the carboxylation activity is retained
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant Escherichia coli expressing sdc converts 40 mM phenol to 10.6 mM salicylate with a 27% (mol/mol) yield at 30°C for 9 h
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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selective and ecological production by carboxylation of phenol to form salicylate, the enzymatic Kolbe–Schmitt reaction
synthesis
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selective and ecological production by carboxylation of phenol to form salicylate, the enzymatic Kolbe–Schmitt reaction
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.91)
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