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Difference between revisions of "Glycoside Hydrolase Family 43"
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== 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 03:49, 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].