Literature summary for 3.2.1.150 extracted from

Yaoi, K.; Kondo, H.; Hiyoshi, A.; Noro, N.; Sugimoto, H.; Tsuda, S.; Mitsuishi, Y.; Miyazaki, K.
The structural basis for the exo-mode of action in GH74 oligoxyloglucan reducing end-specific cellobiohydrolase (2007), J. Mol. Biol., 370, 53-62.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed in Escherichia coli BL21(DE3) as a His-tagged fusion protein	Geotrichum

Crystallization (Commentary)

Crystallization (Comment)	Organism
by using the hanging-drop vapor-diffusion method. X-ray crystal structure of the OXG-RCBH-substrate complex is determined to a resolution of 2.4 A. OXG-RCBH consists of two seven bladed beta-propeller domains. There is a large cleft between the two domains, and a unique loop encloses one side of the active site cleft. Substrate bound to the cleft, and its reducing end is arranged near the loop region that is believed to impart OXG-RCBH with its activity	Geotrichum

Crystallization (Comment)

Organism

by using the hanging-drop vapor-diffusion method. X-ray crystal structure of the OXG-RCBH-substrate complex is determined to a resolution of 2.4 A. OXG-RCBH consists of two seven bladed beta-propeller domains. There is a large cleft between the two domains, and a unique loop encloses one side of the active site cleft. Substrate bound to the cleft, and its reducing end is arranged near the loop region that is believed to impart OXG-RCBH with its activity

Geotrichum

Protein Variants

Protein Variants	Comment	Organism
D465N	inactive OXG-RCBH is co-crystallized with a heptaxyloglucan substrate (XXXG) under conditions similar to the wild-type. There are no differences in the overall structure between the mutant and the wild-type	Geotrichum
DELTAG375-H385	a deltaloop mutant (deletion mutant of the loop region, Gly375His385) is constructed. The mutant shows endo-activity with altered substrate recognition. More specifically, cleavage occurs randomly instead of at specific sites, most likely due to the misalignment of the substrate within the subsite. It is supposed that the loop imparts unique substrate specificity with exo-mode hydrolysis in OXG-RCBH	Geotrichum

Organism

Organism	UniProt	Comment	Textmining
Geotrichum	-	sp. M128	-

Purification (Commentary)

Purification (Comment)	Organism
purified by using a HiTrap DEAE FF column	Geotrichum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
xyloglucan tetradecasaccharide	enzyme substrate specificity to the tetradecasaccharide, XXXGXXXG, is analyzed. Wild-type OXG-RCBH generates XXXGXX and XG due to its strict specificity	Geotrichum	?	-	?

Synonyms

Synonyms	Comment	Organism
oligoxyloglucan reducing end-specific cellobiohydrolase	-	Geotrichum
OXG-RCBH	-	Geotrichum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
45	-	assay at	Geotrichum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	assay at	Geotrichum