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 54"

From CAZypedia
Jump to navigation Jump to search
Line 36: Line 36:
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
The first solved 3-D structure was &alpha;-L-arabinofuranosidase B (AkAbfB) from ''Aspergillus kawachii'' IFO 4308 (http://www.rcsb.org/pdb/explore/explore.do?structureId=1WD3 PDB 1wd3) in 2004 <cite>REF1</cite>.
+
The first solved 3-D structure was &alpha;-L-arabinofuranosidase B (AkAbfB) from ''Aspergillus kawachii'' IFO 4308 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1WD3 PDB 1wd3]) in 2004 <cite>REF1</cite>.
  
 
== Carbohydrate-Binding Module ==
 
== Carbohydrate-Binding Module ==
Line 45: Line 45:
 
;First catalytic nucleophile identification:  
 
;First catalytic nucleophile identification:  
 
;First general acid/base residue identification:
 
;First general acid/base residue identification:
;First 3-D structure: &alpha;-L-Arabinofuranosidase B (AkAbfB) from ''Aspergillus kawachii'' IFO 4308 (http://www.rcsb.org/pdb/explore/explore.do?structureId=1WD3 PDB 1wd3) <cite>REF1</cite>.
+
;First 3-D structure: &alpha;-L-Arabinofuranosidase B (AkAbfB) from ''Aspergillus kawachii'' IFO 4308 ([http://www.rcsb.org/pdb/explore/explore.do?structureId=1WD3 PDB 1wd3]) <cite>REF1</cite>.
  
 
== References ==
 
== References ==

Revision as of 04:51, 1 July 2009


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. Binding to arabinofuranose (present in arabinoxylan) has been demonstrated [2].

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 | PubMed ID:15292273 [REF1]
  2. 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 | PubMed ID:16846393 [REF2]

All Medline abstracts: PubMed