Literature summary for 4.1.1.91 extracted from

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 (2010), Biochem. Biophys. Res. Commun., 394, 279-284.

Search for more literature for 4.1.1.91

Application

Application	Comment	Organism
synthesis	selective and ecological production by carboxylation of phenol to form salicylate, the enzymatic KolbeSchmitt reaction	Cutaneotrichosporon moniliiforme

Cloned(Commentary)

Cloned (Comment)	Organism
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	Cutaneotrichosporon moniliiforme

Inhibitors

Inhibitors	Comment	Organism	Structure
AgNO3	1 mM, complete loss of decarboxylation activity, 60% loss of carboxylation activity	Cutaneotrichosporon moniliiforme
CuCl2	1 mM, 70% loss of carboxylation activity, 14% loss of decarboxylation activity	Cutaneotrichosporon moniliiforme
diethyl dicarbonate	1 mM, 37% inhibition of carboxylation activity, 21% inhibition of decarboxylation activity	Cutaneotrichosporon moniliiforme
HgCl2	1 mM, complete inhibition of decarboxylation activity, 94% loss of carboxylation activity	Cutaneotrichosporon moniliiforme
hydroxylamine	1 mM, 23% inhibition of carboxylation activity, 9% inhibition of decarboxylation activity	Cutaneotrichosporon moniliiforme
additional information	the enzyme is oxygen-insensitive	Cutaneotrichosporon moniliiforme
NEM	1 mM, 28% loss of carboxylation activity, 6% loss of decarboxylation activity	Cutaneotrichosporon moniliiforme
NiCl2	1 mM, 85% loss carboxylation activity, 46% loss of decarboxylation activity	Cutaneotrichosporon moniliiforme
p-chloromercuribenzoic acid	0.2 mM, 49% loss of carboxylation activity, 82% loss of decarboxylation activity	Cutaneotrichosporon moniliiforme

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.08	-	salicylate	pH 5.5, 40°C	Cutaneotrichosporon moniliiforme
123	-	phenol	pH 5.5, 30°C	Cutaneotrichosporon moniliiforme

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	1 mM, 1.5fold stimulation of carboxylation activity, no effect on decarboxylation activity	Cutaneotrichosporon moniliiforme

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40000	-	4 * 40000, SDS-PAGE	Cutaneotrichosporon moniliiforme
140000	-	gel filtration	Cutaneotrichosporon moniliiforme

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
salicylate	Cutaneotrichosporon moniliiforme	-	phenol + CO2	-	?
salicylate	Cutaneotrichosporon moniliiforme WU-0401	-	phenol + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Cutaneotrichosporon moniliiforme	-	-	-
Cutaneotrichosporon moniliiforme WU-0401	-	-	-

Oxidation Stability

Oxidation Stability	Organism
the enzyme is oxygen insensitive	Cutaneotrichosporon moniliiforme

Purification (Commentary)

Purification (Comment)	Organism
-	Cutaneotrichosporon moniliiforme

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.47	-	pH 5.5, 40°C, production of phenol from salicylic acid	Cutaneotrichosporon moniliiforme

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2,3-dihydroxybenzoate	-	Cutaneotrichosporon moniliiforme	1,2-dihydroxybenzene + CO2	i.e. catechol	r
2,3-dihydroxybenzoate	-	Cutaneotrichosporon moniliiforme WU-0401	1,2-dihydroxybenzene + CO2	i.e. catechol	r
2,4-dihydroxybenzoate	i.e beta-resorcylic acid	Cutaneotrichosporon moniliiforme	1,3-dihydroxybenzene + CO2	i.e. resorcinol	r
2,4-dihydroxybenzoate	i.e beta-resorcylic acid	Cutaneotrichosporon moniliiforme WU-0401	1,3-dihydroxybenzene + CO2	i.e. resorcinol	r
2,6-dihydroxybenzoate	i.e gamma-resorcylic acid	Cutaneotrichosporon moniliiforme	1,3-dihydroxybenzene + CO2	i.e. resorcinol	r
4-aminosalicylate	-	Cutaneotrichosporon moniliiforme	3-aminophenol + CO2	-	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	Cutaneotrichosporon moniliiforme	?	-	?
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	Cutaneotrichosporon moniliiforme WU-0401	?	-	?
salicylate	-	Cutaneotrichosporon moniliiforme	phenol + CO2	-	?
salicylate	in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid	Cutaneotrichosporon moniliiforme	phenol + CO2	-	r
salicylate	-	Cutaneotrichosporon moniliiforme WU-0401	phenol + CO2	-	?
salicylate	in the reverse direction the enzyme catalyses the regioselective carboxylation of phenol into stoichiometric amounts of salicylic acid	Cutaneotrichosporon moniliiforme WU-0401	phenol + CO2	-	r

Subunits

Subunits	Comment	Organism
homotetramer	4 * 40000, SDS-PAGE	Cutaneotrichosporon moniliiforme

Synonyms

Synonyms	Comment	Organism
salicylic acid decarboxylase	-	Cutaneotrichosporon moniliiforme
SCD	-	Cutaneotrichosporon moniliiforme

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	carboxylation activity	Cutaneotrichosporon moniliiforme
40	-	assay at, decarboxylation activity	Cutaneotrichosporon moniliiforme

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
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	Cutaneotrichosporon moniliiforme

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	-	1 h, carboxylation activity is stable up to	Cutaneotrichosporon moniliiforme
40	-	1 h, decarboxylation activity is stable up to, 60% of the carboxylation activity is retained	Cutaneotrichosporon moniliiforme
50	-	1 h, 40% of the decarboxylation activity is retained	Cutaneotrichosporon moniliiforme

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.034	-	salicylate	pH 5.5, 40°C	Cutaneotrichosporon moniliiforme
1.1	-	phenol	pH 5.5, 30°C	Cutaneotrichosporon moniliiforme

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	production of phenol from salicylate	Cutaneotrichosporon moniliiforme

pH Range

pH Minimum	pH Maximum	Comment	Organism
5	8.5	pH 5.0: about 75% of maximal activity, pH 8.5: about 50% of maximal activity, production of phenol from salicylate	Cutaneotrichosporon moniliiforme

Cofactor

Cofactor	Comment	Organism	Structure
additional information	the enzyme does not require pyridoxal 5'-phosphate, NADH, and NADPH	Cutaneotrichosporon moniliiforme

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)