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Glycoside Hydrolase Family 54
| Glycoside Hydrolase Family 54 | |
| Clan | none |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH54.html | |
Substrate specificities
This family contains α-L-arabinofuranosidase (EC 3.2.1.55) and β-xylosidase (EC 3.2.1.37).
Kinetics and Mechanism
GH54 members are retaining enzymes.
Catalytic Residues
Three-dimensional structures
The first solved 3-D structure was α-L-arabinofuranosidase B (AkAbfB) from Aspergillus kawachii IFO 4308 (PDB 1wd3) in 2004 [1].
Carbohydrate-Binding Module
Most of the members in GH54 have Carbohydrate-Binding Module Family 42 of approx. 160 residues at the C-terminus of GH54 catalytic domains. This module was firstly found as a xylan binding domain [2], and binding to arabinofuranose (present in arabinoxylan) has been subsequently demonstrated [3].
Family Firsts
- First sterochemistry determination
- Cite some reference here, with a short explanation.
- First catalytic nucleophile identification
- First general acid/base residue identification
- First 3-D structure
- α-L-Arabinofuranosidase B (AkAbfB) from Aspergillus kawachii IFO 4308 by X-ray crystallography (PDB 1wd3 and PDB 1wd4) [1].
References
- Miyanaga A, Koseki T, Matsuzawa H, Wakagi T, Shoun H, and Fushinobu S. (2004). Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose. J Biol Chem. 2004;279(43):44907-14. DOI:10.1074/jbc.M405390200 |
- Nogawa M, Yatsui K, Tomioka A, Okada H, and Morikawa Y. (1999). An alpha-L-arabinofuranosidase from Trichoderma reesei containing a noncatalytic xylan-binding domain. Appl Environ Microbiol. 1999;65(9):3964-8. DOI:10.1128/AEM.65.9.3964-3968.1999 |
- Miyanaga A, Koseki T, Miwa Y, Mese Y, Nakamura S, Kuno A, Hirabayashi J, Matsuzawa H, Wakagi T, Shoun H, and Fushinobu S. (2006). The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose. Biochem J. 2006;399(3):503-11. DOI:10.1042/BJ20060567 |