Welcome to the Carbohydrate-Active enZYmes Database

The March 2023 update of CAZy!

The March update includes the novel GH31 subclassification by S. Williams’ team (PMID=36806678), after the January release of subfamilies for the GH19, GH45, GH51, GH55, GH68 and GH130 families (accepted in PLOS Computational Biology).
Further, we created 9 novel families : CBM95 to CBM97 and GH175 to GH180, while at least 3 additional new GH families are already expected in the our next update, based on these works about to be published: doi=10.1101/2022.07.22.500997 and doi=10.1101/2022.07.22.500997.

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 !

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

welan gum lyase (WelR; ATB93_17710)KTF67430.14.2.2.- pubmed
b-1,3-xylanase (Xyl88)WP_052432230. pubmed
b-1,3-xylanase (Xyl512)WP_052431877. pubmed
b-1,3-xylanase (Xyn80)WP_253969254. pubmed
M-specific alginate lyase (paeh-aly)WP_127487869.
b-1,3-xylanase (Xyn65)WP_253968372. pubmed
b-D-galactofuranosidase (BACFIN_08810)EEX43527.
exo-a-1,5-D-arabinofuranosidase (HMPREF9455_02479; DgGH172c)EGK01287.13.2.1.-doi
exo-a-1,5-D-arabinofuranosidase (HMPREF9455_02471;DgGH172b)EGK01279.13.2.1.-doi
[ginsenoside] b-xylosidase (StGH43; STRTUCAR8_01029)ELP66521. pubmed
neuraminidaseAVM87625. pubmed
dextransucraseWP_028291708. pubmed
ascorbate peroxidase (PVAP13_9KG480900)KAG2552739. pubmed
pullulanase 1, chloroplastic (MePUL;Loc110624912)XP_021626046.
3-O-methylmannan endo-a-1,4-mannosidase (MmpH; MHAS_04404)VCT92674.13.2.1.- pubmed
Last update: 2023-03-08 © Copyright 1998-2023
AFMB - CNRS - Université d'Aix-Marseille