CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.
Difference between revisions of "Glycoside Hydrolase Family 43"
Line 28: | Line 28: | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
− | + | NMR, deploying arabinan as the substrate, showed that an endo-alpha1,5-arabinanase displays a single displacement or inverting mechanism | |
− | |||
== Catalytic Residues == | == Catalytic Residues == |
Revision as of 04:49, 18 June 2009
- Author: Satoshi Kaneko
- Responsible Editor: Harry Brumer
Glycoside Hydrolase Family GH43 | |
Clan | GH-F |
Mechanism | inverting |
Active site residues | not known |
CAZy DB link | |
http://www.cazy.org/fam/GH43.html |
Substrate specificities
GH43 enzymes display a variety of exo-activities in which L-arabinofuanose, D-galactopyranose and D-xylopyranose residues are hydrolyzed from the non-reducing end of polysacchrides or aryl groups. In addition examples of endo-alpha1,5-arabinanases are also evident in this family
Kinetics and Mechanism
NMR, deploying arabinan as the substrate, showed that an endo-alpha1,5-arabinanase displays a single displacement or inverting mechanism
Catalytic Residues
Three-dimensional structures
Family Firsts
- First sterochemistry determination
- First catalytic nucleophile identification
- First general acid/base residue identification
- First 3-D structure
- alpha-L-Arabinanase from Cellvibrio japonicus [1].