Information on EC 4.1.1.91 - salicylate decarboxylase

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The expected taxonomic range for this enzyme is: Trichosporon moniliiforme

EC NUMBER
COMMENTARY hide
4.1.1.91
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RECOMMENDED NAME
GeneOntology No.
salicylate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
salicylate = phenol + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
salicylate degradation III
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain WU-0401
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Manually annotated by BRENDA team
strain WU-0401
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
show the reaction diagram
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
show the reaction diagram
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
show the reaction diagram
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i.e gamma-resorcylic acid
i.e. resorcinol
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r
4-aminosalicylate
3-aminophenol + CO2
show the reaction diagram
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r
salicylate
phenol + CO2
show the reaction diagram
additional information
?
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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
salicylate
phenol + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
Fe2+
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1 mM, 1.5fold stimulation of carboxylation activity, no effect on decarboxylation activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
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the enzyme is oxygen-insensitive
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
123
phenol
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pH 5.5, 30°C
1.08
salicylate
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pH 5.5, 40°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
phenol
Trichosporon moniliiforme
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pH 5.5, 30°C
0.034
salicylate
Trichosporon moniliiforme
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pH 5.5, 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.47
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pH 5.5, 40°C, production of phenol from salicylic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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production of phenol from salicylate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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carboxylation activity
40
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assay at, decarboxylation activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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4 * 40000, SDS-PAGE
140000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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1 h, carboxylation activity is stable up to
40
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1 h, decarboxylation activity is stable up to, 60% of the carboxylation activity is retained
50
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1 h, 40% of the decarboxylation activity is retained
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is oxygen insensitive
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707400
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 hide
LITERATURE
synthesis