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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.37 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

EC Number Inhibitors Comment Organism Structure
3.2.1.37 D-xylose
-
 Geobacillus thermoleovorans
3.2.1.37 L-arabinose
-
 Geobacillus thermoleovorans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.37 Geobacillus thermoleovorans Q2I2N4
-
-
3.2.1.37 Geobacillus thermoleovorans IT-08 Q2I2N4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.37
-
 Geobacillus thermoleovorans

Synonyms

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