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Information on EC 4.1.1.91 - salicylate decarboxylase
for references in articles please use BRENDA:EC4.1.1.91
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IUBMB Comments
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 .
The expected taxonomic range for this enzyme is: Cutaneotrichosporon moniliiforme
showSynonyms
salicylic acid decarboxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
salicylic acid decarboxylase
SCD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
salicylate = phenol + CO2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dihydroxybenzene + CO2
2,3-dihydroxybenzoate
Substrates: -
Products: -
Products: -
r
1,3-dihydroxybenzene + CO2
2,4-dihydroxybenzoate
Substrates: -
Products: -
Products: -
r
1,3-dihydroxybenzene + CO2
2,6-dihydroxybenzoate
Substrates: -
Products: -
Products: -
r
4-aminosalicylate
3-aminophenol + CO2
-
Substrates: -
Products: -
Products: -
r
ginkgolic acid C15:1
3-(8Z-pentadecenyl)-phenol + CO2
Substrates: -
Products: -
Products: -
?
ginkgolic acid C15:1
3-[(8Z)-pentadecenyl]phenol + CO2
Substrates: -
Products: -
Products: -
?
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
-
Substrates: -
Products: i.e. catechol
Products: i.e. catechol
r
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
Substrates: -
Products: -
Products: -
r
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
-
Substrates: -
Products: i.e. catechol
Products: i.e. catechol
r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
-
Substrates: i.e beta-resorcylic acid
Products: i.e. resorcinol
Products: i.e. resorcinol
r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
Substrates: -
Products: -
Products: -
r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
-
Substrates: i.e beta-resorcylic acid
Products: i.e. resorcinol
Products: i.e. resorcinol
r
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
-
Substrates: i.e gamma-resorcylic acid
Products: i.e. resorcinol
Products: i.e. resorcinol
r
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
Substrates: -
Products: -
Products: -
r
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
-
Substrates: i.e gamma-resorcylic acid
Products: i.e. resorcinol
Products: i.e. resorcinol
r
salicylate
phenol + CO2
-
Substrates: in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid
Products: -
Products: -
r
salicylate
phenol + CO2
-
Substrates: -
Products: -
Products: -
?
salicylate
phenol + CO2
-
Substrates: in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid
Products: -
Products: -
r
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates for decarboxylation: 3-hydroxybenzoate, 4-hydroxybenzoate, 3,4-dihydroxybenzoate, or 3,5-dihydroxybenzoate
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
salicylate
phenol + CO2
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme does not require pyridoxal 5'-phosphate, NADH, and NADPH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
1 mM, 1.5fold stimulation of carboxylation activity, no effect on decarboxylation activity
Mg2+
Zn2+
Mg2+
SDC is a Mg-dependent enzyme rather than the Zn2+-dependent, and the substrate is bidentately coordinated to the metal center in the catalysis
Zn2+
highest relative activity is observed in the presence of Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AgNO3
-
1 mM, complete loss of decarboxylation activity, 60% loss of carboxylation activity
CuCl2
-
1 mM, 70% loss of carboxylation activity, 14% loss of decarboxylation activity
diethyl dicarbonate
-
1 mM, 37% inhibition of carboxylation activity, 21% inhibition of decarboxylation activity
HgCl2
-
1 mM, complete inhibition of decarboxylation activity, 94% loss of carboxylation activity
hydroxylamine
-
1 mM, 23% inhibition of carboxylation activity, 9% inhibition of decarboxylation activity
NEM
-
1 mM, 28% loss of carboxylation activity, 6% loss of decarboxylation activity
NiCl2
-
1 mM, 85% loss carboxylation activity, 46% loss of decarboxylation activity
p-chloromercuribenzoic acid
-
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
0.47
2,3-Dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
1.2
2,4-Dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
11
2,6-dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
0.046
ginkgolic acid C15:1
pH not specified in the publication, 40°C
0.227
ginkgolic acid C15:1
mutant P191A, pH 5.5, 40°C
0.5 - 2
salicylate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
0.65
salicylate
mutant Y64T/P191G/E302D, pH 5.5, 40°C
0.68
salicylate
mutant Y64T/P191G/F195V, pH 5.5, 40°C
0.72
salicylate
mutant Y64T/F195V/E302D, pH 5.5, 40°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
46
2,3-Dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
2 - 8
2,4-Dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
5.2
2,6-dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
0.0093
ginkgolic acid C15:1
mutant Y64T, pH 5.5, 40°C
0.0118
ginkgolic acid C15:1
mutant P191A, pH 5.5, 40°C
44
salicylate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
98
2,3-Dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
22
2,4-Dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
0.46
2,6-dihydroxybenzoate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
0.052
ginkgolic acid C15:1
mutant P191A, pH 5.5, 40°C
84
salicylate
mutant Y64T/P191G/F195V/E302D, pH 5.5, 40°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.47
-
pH 5.5, 40°C, production of phenol from salicylic acid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
-
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
30
40
50
50
wild-type and mutant P191A, substrate ginkgolic acid C15:1
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
-
20°C: about 35% of maximal activity, 30°C: maximal activity, 40°C: about 10% of maximal activity, production of salicylate from phenol
35 - 60
more than 80% of maximum decarboxylation activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
enzyme follows the general mechanism of amidohydrolase superfamily decarboxylases. The reaction begins with proton transfer from a metal-coordinated aspartic acid residue (Asp298 in SDC) to the C1 of salicylic acid, which is followed by the C-C bond cleavage, to generate the phenol product and release CO2
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and molecular docking of substrates salicylic acid and ginkgolic acid C15:1
the conserved residues of Glu8, His169, and Asp298 are the catalytic residues within the TIM-barrel. Trp239 forms a hydrophobic recognition site by interacting with the phenyl ring of salicylic acid, while Arg235 is responsible for recognizing the hydroxyl group at the C2 of salicylic acid via hydrogen bond interactions
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P191A
decarboxylation activity increased by 1116.7% for substrate ginkgolic acid C15:1
Y64T
Y64T/P191G/F195V
15.6fold increase in catalytic activity
Y64T/P191G/F195V/E302D
26.4fold increase in kcat/Km compared with the wild-type
Y64T
decarboxylation activity increased by 105.18% for substrate ginkgolic acid C15:1
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
1 h, decarboxylation activity is stable up to, 60% of the carboxylation activity is retained
50
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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
-
selective and ecological production by carboxylation of phenol to form salicylate, the enzymatic KolbeSchmitt reaction
synthesis
-
selective and ecological production by carboxylation of phenol to form salicylate, the enzymatic KolbeSchmitt reaction
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kirimura, K.; Gunji, H.; Wakayama, R.; Hattori, T.; Ishii, Y.
Enzymatic Kolbe-Schmitt reaction to form salicylic acid from phenol: enzymatic characterization and gene identification of a novel enzyme, Trichosporon moniliiforme salicylic acid decarboxylase
Biochem. Biophys. Res. Commun.
394
279-284
2010
Cutaneotrichosporon moniliiforme, Cutaneotrichosporon moniliiforme WU-0401
brenda
Hu, Y.; Hua, Q.; Sun, G.; Shi, K.; Zhang, H.; Zhao, K.; Jia, S.; Dai, Y.; Wu, Q.
The catalytic activity for ginkgolic acid biodegradation, homology modeling and molecular dynamic simulation of salicylic acid decarboxylase
Comput. Biol. Chem.
75
82-90
2018
Cutaneotrichosporon moniliiforme (P0CT50)
brenda
Chen, F.; Zhao, Y.; Zhang, C.; Wang, W.; Gao, J.; Li, Q.; Qin, H.; Dai, Y.; Liu, W.; Liu, F.; Su, H.; Sheng, X.
A combined computational-experimental study on the substrate binding and reaction mechanism of salicylic acid decarboxylase
Catalysts
12
1577
2022
Cutaneotrichosporon moniliiforme (P0CT50)
-
brenda
Gao, X.; Wu, M.; Zhang, W.; Li, C.; Guo, R.T.; Dai, Y.; Liu, W.; Mao, S.; Lu, F.; Qin, H.M.
Structural basis of salicylic acid decarboxylase reveals a unique substrate recognition mode and access channel
J. Agric. Food Chem.
69
11616-11625
2021
Cutaneotrichosporon moniliiforme (P0CT50)
brenda
Song, Y.; Hu, Y.; Li, J.; Wang, L.; Jing, W.; Zhang, L.; Dai, Y.; Jia, S.; Meng, X.; Zhang, H.
Site-directed mutation of salicylate decarboxylase gene and mechanism of ginkgo acid decarboxylation
Protein J.
42
1-13
2023
Cutaneotrichosporon moniliiforme (P0CT50)
brenda
EXTERNAL LINKS (specific for EC-Number 4.1.1.91)
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