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Literature summary for 3.2.1.67 extracted from

  • Pijning, T.; van Pouderoyen, G.; Kluskens, L.; van der Oost, J.; Dijkstra, B.W.
    The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer (2009), FEBS Lett., 583, 3665-3670.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with substrate, hanging drop vapour diffusion method, 20°C, mixing of 0.0015 ml of protein solution containing 12 mg/ml in 10 mM HEPES-NaOH, pH 7.5, and 3 mM NaN3 with 0.0015 ml of reservoir solution containing 10-17% w/v PEG 4000, 0.1 M BES–NaOH, pH 6.5, cryoprotection by 17% w/v PEG 4000, 10% v/v PEG 400, 0.1 MBES–NaOH, pH 6.5, X-ray diffraction structure determination and analysis at 2.05 A resolution, molecular replacement Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
polygalacturonic acid + H2O Thermotoga maritima
-
galacturonic acid + ?
-
?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information modelling of substrate binding, and active site structure, overview Thermotoga maritima ?
-
?
polygalacturonic acid + H2O
-
Thermotoga maritima galacturonic acid + ?
-
?
tetragalacturonic acid + H2O modelling of substrate binidng, structure, overview Thermotoga maritima galacturonic acid + trigalacturonic acid
-
?

Subunits

Subunits Comment Organism
tetramer quaternary structure, overview Thermotoga maritima

Synonyms

Synonyms Comment Organism
exoPG
-
Thermotoga maritima
exopolygalacturonase
-
Thermotoga maritima
More the enzyme belongs to the glycosyl hydrolase family 28, GH28 Thermotoga maritima