Glycoside Hydrolase Family 54

• Author: Shinya Fushinobu
• Responsible Curator: Shinya Fushinobu

---

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.

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 (PDB 1wd3) [1].

References

1. 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 |
2. 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 |
3. 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 |