Skip Navigation



Nucleic Acids Research Advance Access published online on October 5, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn663
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (1381K) Freely available
Right arrow Screen PDF (321K) Freely available
Right arrow All Versions of this Article:
37/suppl_1/D233    most recent
gkn663v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Cantarel, B. L.
Right arrow Articles by Henrissat, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cantarel, B. L.
Right arrow Articles by Henrissat, B.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Database Issue

The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

Brandi L. Cantarel, Pedro M. Coutinho, Corinne Rancurel, Thomas Bernard, Vincent Lombard and Bernard Henrissat*

Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS, Universités Aix-Marseille I & II, 163 Avenue de Luminy, 13288 Marseille, France

*To whom correspondence should be addressed. Tel: +33 4 91 82 55 87; Fax: +33 491 26 67 20; Email: Bernard.Henrissat{at}afmb.univ-mrs.fr

Correspondence may also be addressed to Pedro M. Coutinho. Email: Pedro.Coutinho{at}afmb.univ-mrs.fr

Received September 15, 2008. Accepted September 19, 2008.

The Carbohydrate-Active Enzyme (CAZy) database is a knowledge-based resource specialized in the enzymes that build and breakdown complex carbohydrates and glycoconjugates. As of September 2008, the database describes the present knowledge on 113 glycoside hydrolase, 91 glycosyltransferase, 19 polysaccharide lyase, 15 carbohydrate esterase and 52 carbohydrate-binding module families. These families are created based on experimentally characterized proteins and are populated by sequences from public databases with significant similarity. Protein biochemical information is continuously curated based on the available literature and structural information. Over 6400 proteins have assigned EC numbers and 700 proteins have a PDB structure. The classification (i) reflects the structural features of these enzymes better than their sole substrate specificity, (ii) helps to reveal the evolutionary relationships between these enzymes and (iii) provides a convenient framework to understand mechanistic properties. This resource has been available for over 10 years to the scientific community, contributing to information dissemination and providing a transversal nomenclature to glycobiologists. More recently, this resource has been used to improve the quality of functional predictions of a number genome projects by providing expert annotation. The CAZy resource resides at URL: http://www.cazy.org/.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J R Soc InterfaceHome page
C. E. French
Synthetic biology and biomass conversion: a match made in heaven?
J R Soc Interface, August 6, 2009; 6(Suppl_4): S547 - S558.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
N. Heise, D. Singh, H. van der Wel, S. O Sassi, J. M Johnson, C. L Feasley, C. M Koeller, J. O Previato, L. Mendonca-Previato, and C. M West
Molecular analysis of a UDP-GlcNAc:polypeptide {alpha}-N-acetylglucosaminyltransferase implicated in the initiation of mucin-type O-glycosylation in Trypanosoma cruzi
Glycobiology, August 1, 2009; 19(8): 918 - 933.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Nakajima, M. Nishimoto, and M. Kitaoka
Characterization of Three {beta}-Galactoside Phosphorylases from Clostridium phytofermentans: DISCOVERY OF D-GALACTOSYL-{beta}1->4-L-RHAMNOSE PHOSPHORYLASE
J. Biol. Chem., July 17, 2009; 284(29): 19220 - 19227.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Brazier-Hicks, K. M. Evans, M. C. Gershater, H. Puschmann, P. G. Steel, and R. Edwards
The C-Glycosylation of Flavonoids in Cereals
J. Biol. Chem., July 3, 2009; 284(27): 17926 - 17934.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Maruyama, Y. Nakamichi, T. Itoh, B. Mikami, W. Hashimoto, and K. Murata
Substrate Specificity of Streptococcal Unsaturated Glucuronyl Hydrolases for Sulfated Glycosaminoglycan
J. Biol. Chem., July 3, 2009; 284(27): 18059 - 18069.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
A. Vanden Wymelenberg, J. Gaskell, M. Mozuch, P. Kersten, G. Sabat, D. Martinez, and D. Cullen
Transcriptome and Secretome Analyses of Phanerochaete chrysosporium Reveal Complex Patterns of Gene Expression
Appl. Envir. Microbiol., June 15, 2009; 75(12): 4058 - 4068.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
D. Dodd, S. A. Kocherginskaya, M. A. Spies, K. E. Beery, C. A. Abbas, R. I. Mackie, and I. K. O. Cann
Biochemical Analysis of a {beta}-D-Xylosidase and a Bifunctional Xylanase-Ferulic Acid Esterase from a Xylanolytic Gene Cluster in Prevotella ruminicola 23
J. Bacteriol., May 15, 2009; 191(10): 3328 - 3338.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Carapito, A. Imberty, J.-M. Jeltsch, S. C. Byrns, P.-H. Tam, T. L. Lowary, A. Varrot, and V. Phalip
Molecular Basis of Arabinobio-hydrolase Activity in Phytopathogenic Fungi: CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF FUSARIUM GRAMINEARUM GH93 EXO-{alpha}-L-ARABINANASE
J. Biol. Chem., May 1, 2009; 284(18): 12285 - 12296.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. A. Mahowald, F. E. Rey, H. Seedorf, P. J. Turnbaugh, R. S. Fulton, A. Wollam, N. Shah, C. Wang, V. Magrini, R. K. Wilson, et al.
Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla
PNAS, April 7, 2009; 106(14): 5859 - 5864.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.