Literature summary for 3.2.1.37 extracted from

Rohman, A.; van Oosterwijk, N.; Puspaningsih, N.N.T.; Dijkstra, B.W.
Structural basis of product inhibition by arabinose and xylose of the thermostable GH43 beta-1,4-xylosidase from Geobacillus thermoleovorans IT-08 (2018), PLoS ONE, 13, e0196358 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor-diffusion method at 10°C, crystal structures of the enzyme in the unliganded form and with bound products, at 1.7 A resolution. The structures are very similar to those of other enzymes belonging to glycoside hydrolase family 43. The monosaccharides are bound in very different ways. Arabinose preferentially binds in subsite -1, while xylose exclusively interacts with subsite +1	Geobacillus thermoleovorans

Crystallization (Comment)

Organism

hanging-drop vapor-diffusion method at 10°C, crystal structures of the enzyme in the unliganded form and with bound products, at 1.7 A resolution. The structures are very similar to those of other enzymes belonging to glycoside hydrolase family 43. The monosaccharides are bound in very different ways. Arabinose preferentially binds in subsite -1, while xylose exclusively interacts with subsite +1

Geobacillus thermoleovorans

Inhibitors

Inhibitors	Comment	Organism	Structure
D-xylose	-	Geobacillus thermoleovorans
L-arabinose	-	Geobacillus thermoleovorans

Organism

Organism	UniProt	Comment	Textmining
Geobacillus thermoleovorans	Q2I2N4	-	-
Geobacillus thermoleovorans IT-08	Q2I2N4	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Geobacillus thermoleovorans

Synonyms

Synonyms	Comment	Organism
beta-1,4-xylosidase	-	Geobacillus thermoleovorans
GH43 beta-1,4-xylosidase	-	Geobacillus thermoleovorans

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Release 2023.1 (January 2023)