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Literature summary extracted from

  • Sheng, X.; Patskovsky, Y.; Vladimirova, A.; Bonanno, J.B.; Almo, S.C.; Himo, F.; Raushel, F.M.
    Mechanism and structure of gamma-resorcylate decarboxylase (2018), Biochemistry, 57, 3167-3175 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.103
-
 Polaromonas sp. JS666

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.103 incomplex with inhibitor 2-nitroresorcinol. 2-NR is directly ligated to a Mn2+ bound in the active site, and the nitro substituent of the inhibitor is tilted significantly from the plane of the phenyl ring Polaromonas sp. JS666

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.103 2-nitroresorcinol
-
 Polaromonas sp. JS666

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.103 0.032
-
 2,6-dihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 0.048
-
 2,4,6-Trihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 0.079
-
 2,6-dihydroxy-4-methylbenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 0.111
-
 2,3-Dihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.103 Mn2+ presence of Mn2+ in the active site, data from crystal structure Polaromonas sp. JS666

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.103 Polaromonas sp. JS666 Q12BV1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.103 2,3-Dihydroxybenzoate
-
 Polaromonas sp. JS666 Catechol + CO2
-
 ?
4.1.1.103 2,4,6-trihydroxybenzoate
-
 Polaromonas sp. JS666 benzene-1,3,5-triol + CO2
-
 ?
4.1.1.103 2,6-dihydroxy-4-methylbenzoate
-
 Polaromonas sp. JS666 resveratrol + CO2
-
 ?
4.1.1.103 2,6-dihydroxybenzoate
-
 Polaromonas sp. JS666 1,3-dihydroxybenzene + CO2
-
 ?
4.1.1.103 additional information in the proposed reaction mechanism, gamma-resorcylate binds 2,6-dihydroxybenzoate by direct coordination of the active site manganese ion to the carboxylate anion of the substrate and one of the adjacent phenolic oxygens. The enzyme subsequently catalyzes the transfer of a proton to C1 of gamma-resorcylate prior to the actual decarboxylation step Polaromonas sp. JS666 ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.103 0.18
-
 2,4,6-Trihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 0.38
-
 2,6-dihydroxy-4-methylbenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 0.44
-
 2,6-dihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 0.47
-
 2,3-Dihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.103 3.8
-
 2,4,6-Trihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 4.2
-
 2,3-Dihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 4.8
-
 2,6-dihydroxy-4-methylbenzoate pH 7.0, 30°C Polaromonas sp. JS666
4.1.1.103 13
-
 2,6-dihydroxybenzoate pH 7.0, 30°C Polaromonas sp. JS666