Welcome to the Carbohydrate-Active enZYmes Database

The March 2024 update of CAZy

This month, we would like to highlight 17 bacterial polysaccharide polymerase families, GT119 to GT135, long-overdue but which required in-depth sequence analyses realized by Meitil and coworkers.

The CAZy database describes the families of structurally-related catalytic and carbohydrate-binding modules (or functional domains) of enzymes that degrade, modify, or create glycosidic bonds.

Online since 1998, CAZy is a specialist database dedicated to the display and analysis of genomic, structural and biochemical information on Carbohydrate-Active Enzymes (CAZymes).

CAZy data are accessible either by browsing sequence-based families or by browsing the content of genomes in carbohydrate-active enzymes. New genomes are added regularly shortly after they appear in the daily releases of GenBank.
New families are created based on published evidence for the activity of at least one member of the family and all families are regularly updated, both in content and in description.

An original aspect of the CAZy database is its attempt to cover all carbohydrate-active enzymes across organisms and across subfields of glycosciences. Please let us know if some families have escaped our attention, we will be happy to add them !

CAZy has developed a platform facility that provides analysis and curation services for your data. If you are interested, please visit CAZy bioinformatics web page and contact : cazy@univ-amu.fr.

For a more extensive encyclopedic resource on the particular features of carbohydrate active enzymes, please visit CAZypedia, a web site driven by the scientific community that studies these enzymes.

PULDB is a database of Polysaccharide Utilization Loci (PULs) in Bacteroidetes. PULDB displays information on experimentally determined and predicted PULs for a number of Bacteroidetes genomes.

A new reference for the CAZy database : We summarized the recent changes in the CAZy database, and evolution during the last eight years in an article published the Nucleic Acids Research (Database Issue), with a specific focus on functional annotations.
Read the full paper.

Enzyme Classes currently covered

Modules that catalyze the breakdown, biosynthesis or modification of carbohydrates and glycoconjugates :

- Glycoside Hydrolases (GHs) : hydrolysis and/or rearrangement of glycosidic bonds (see CAZypedia definition)

- GlycosylTransferases (GTs) : formation of glycosidic bonds (see definition)

- Polysaccharide Lyases (PLs) : non-hydrolytic cleavage of glycosidic bonds

- Carbohydrate Esterases (CEs) : hydrolysis of carbohydrate esters

- Auxiliary Activities (AAs) : redox enzymes that act in conjunction with CAZymes.

Associated Modules currently covered

Carbohydrate-active enzymes often display a modular structure with non-catalytic modules appended to the enzymes above

- Carbohydrate-Binding Modules (CBMs) : adhesion to carbohydrates

Genome analysis by CAZy

Family distribution and/or protein listings of the carbohydrate-active enzymes and associated proteins identified in genomes

- Genomes by Kingdom :


Last Functions released

alginate lyase (AlyC6’)WP_016791256. pubmed
alginate lyase (AlyC6’)WP_016791256. pubmed
b-glycosidase (TY87_18135)PJE53865.
pubmed pubmed
endoxylanase (denovogenes_5086; IKI06_02965)MBR7030185. pubmed
CelXyn2 / IKP37_07625MBR6042486. pubmed
b-galactosidaseWP_076345996. pubmed
b-galactosidase (Gal; GYB58_00550)MBR9790212. pubmed
exo-b-1,3/4/6-galactanase / a-L-arabinopyranosidase (PpBGal42A)WP_040101590.
pubmed pubmed
bifunctional acetylxylan esterase and feruloyl esterase (DmCE1B; HMPREF9456_02279)EGK06015.
pubmed pubmed
acetylxylan esterase (DmCE6A; HMPREF9456_02270)EGK06006. pubmed
feruloyl esterase (DmCE1A; HMPREF9456_02268)EGK06004. pubmed
mixed-linkage xylan-specific endo-b-1,4-xylanase (PpXyn26A; DX130_15985)REK75131.1
3.2.1.- pubmed
mixed-linkage xylan-specific endo-b-1,4-xylanase (CaXyn26A)WP_077338539.13.2.1.- pubmed
mixed-linkage xylan-specific endo-b-1,4-xylanase (CeXyn26A; M4I21_06905)MCL5245529.1
3.2.1.- pubmed
3-O-b-L-arabinopyranosyl-a-L-arabinofuranosidase (AAfase; MCC10289_0425)WP_065438160.1
3.2.1.- pubmed
Last update: 2024-03-18 © Copyright 1998-2024
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