Literature summary for 3.2.1.145 extracted from

Ishida, T.; Fujimoto, Z.; Ichinose, H.; Igarashi, K.; Kaneko, S.; Samejima, M.
Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium (2009), Acta Crystallogr. Sect. F, 65, 1274-1276.

Search for more literature for 3.2.1.145

Cloned(Commentary)

Cloned (Comment)	Organism
Pc1,3Gal43A, expression in Pichia pastoris as selenmethionine-labeled protein	Phanerodontia chrysosporium

Crystallization (Commentary)

Crystallization (Comment)	Organism
selenomethionine-labeled recombinant Pc1,3Gal43A, hanging-drop vapour-diffusion method, 25°C, the reservoir solution contains 16% w/v PEG 10000, 95 mM ammonium sulfate, 95 mM Bis-Tris, pH 5.5, and 4.8% v/v glycerol, 3-10 days, X-ray diffraction structure determination and analysis at 1.8 A resolution, multiwavelength anomalous dispersion method, since molecular replacement is unsuccessful	Phanerodontia chrysosporium

Organism

Organism	UniProt	Comment	Textmining
Phanerodontia chrysosporium	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant selenmethionine-labeled Pc1,3Gal43A from Pichia pastoris by ultrafiltration, and hydrophobic interaction chromatography	Phanerodontia chrysosporium

Subunits

Subunits	Comment	Organism
More	the enzyme consists of a glycoside hydrolase family 43 catalytic domain and a substrate-binding domain that belongs to carbohydrate-binding module family 35	Phanerodontia chrysosporium

Synonyms

Synonyms	Comment	Organism
exo-beta-1,3-galactanase	-	Phanerodontia chrysosporium
More	the enzyme consists of a glycoside hydrolase family 43 catalytic domain and a substrate-binding domain that belongs to carbohydrate-binding module family 35	Phanerodontia chrysosporium
Pc1,3Gal43A	-	Phanerodontia chrysosporium

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Release 2023.1 (January 2023)