Literature summary for 3.2.1.55 extracted from

Yang, Y.; Sun, J.; Wu, J.; Zhang, L.; Du, L.; Matsukawa, S.; Xie, J.; Wei, D.
Characterization of a novel alpha-L-arabinofuranosidase from Ruminococcus albus 7 and rational design for its thermostability (2016), J. Agric. Food Chem., 64, 7546-7554 .

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Protein Variants

Protein Variants	Comment	Organism
H337K	the mutation prolongs the half-life of thermal inactivation at 50°C 5fold versus the wild type, and the specific activity of this mutant is increased	Ruminococcus albus
K208W	the mutation enhances the half-life of thermal inactivation at 50°C more than 11.1times versus the wild type	Ruminococcus albus

Organism

Organism	UniProt	Comment	Textmining
Ruminococcus albus	-	-	-
Ruminococcus albus 7	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	73.3 units/mg at pH 6.0 and 50 °C	Ruminococcus albus

Synonyms

Synonyms	Comment	Organism
alpha-L-arabinofuranosidase	-	Ruminococcus albus
GH 51 Abf	-	Ruminococcus albus

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Release 2023.1 (January 2023)