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Information on EC 4.1.1.91 - salicylate decarboxylase
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4.1.1.91 salicylate decarboxylaseIUBMB 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 .
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
salicylic acid decarboxylase, SCD, SDC, 
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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
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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
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
-
i.e gamma-resorcylic acid
i.e. resorcinol
-
r
ginkgolic acid C15:1
3-(8Z-pentadecenyl)-phenol + CO2
-
-
-
?
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
-
-
i.e. catechol
-
r
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
-
-
i.e. catechol
-
r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
-
i.e beta-resorcylic acid
i.e. resorcinol
-
r
2,4-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
-
i.e beta-resorcylic acid
i.e. resorcinol
-
r
salicylate
phenol + CO2
-
in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid
-
-
r
salicylate
phenol + CO2
-
in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid
-
-
r
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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 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
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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
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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
0.046
ginkgolic acid C15:1
pH not specified in the publication, 40°C
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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
-
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
-
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
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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). SDC_CUTMO
350
0
39961
Swiss-Prot
other Location (Reliability: 2)
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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
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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
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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 KolbeâSchmitt reaction
synthesis
-
selective and ecological production by carboxylation of phenol to form salicylate, the enzymatic KolbeâSchmitt 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
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