Literature summary extracted from

Ihsanawati, K.; Kumasaka, T.; Kaneko, T.; Morokuma, C.; Yatsunami, R.; Sato, T.; Nakamura, S.; Tanaka, N.
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8 (2005), Proteins, 61, 999-1009.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.2.1.8	in complex with xylotriose and xylobiose	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.8	Thermotoga maritima	-	-	-
3.2.1.8	Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589	-	-	-

Subunits

EC Number	Subunits	Comment	Organism
3.2.1.8	More	enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data	Thermotoga maritima

Synonyms

EC Number	Synonyms	Comment	Organism
3.2.1.8	TmxB	-	Thermotoga maritima

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
3.2.1.8	additional information	-	features that account for the high thermostability of enzyme are clusters of aromatic residues together with a lack of exposed hydrophobic residues	Thermotoga maritima

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Release 2023.1 (January 2023)