Cited by 2,439Genomics and Phylogenetic StudiesEnzyme Production and CharacterizationEnzyme Catalysis and Immobilization

The carbohydrate-active enzyme database: functions and literature

Open access
Drula, Elodie, Garron, Marie-Line, Dogan, Suzan, Lombard, Vincent, Henrissat, Bernard, Terrapon, Nicolas·2022·Nucleic Acids Research

Abstract

Thirty years have elapsed since the emergence of the classification of carbohydrate-active enzymes in sequence-based families that became the CAZy database over 20 years ago, freely available for browsing and download at www.cazy.org. In the era of large scale sequencing and high-throughput Biology, it is important to examine the position of this specialist database that is deeply rooted in human curation. The three primary tasks of the CAZy curators are (i) to maintain and update the family classification of this class of enzymes, (ii) to classify sequences newly released by GenBank and the Protein Data Bank and (iii) to capture and present functional information for each family. The CAZy website is updated once a month. Here we briefly summarize the increase in novel families and the annotations conducted during the last 8 years. We present several important changes that facilitate taxonomic navigation, and allow to download the entirety of the annotations. Most importantly we highlight the considerable amount of work that accompanies the analysis and report of biochemical data from the literature.

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Crossref · 10.1093/nar/gkab1045

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  • NEU1 is part of the GH33 family of glycoside hydrolases.

    “NEU1 is part of the GH33 family of glycoside hydrolases (64), which comprises bacterial and eukaryotic enzymes (65–68) that release terminal sialic acids from glycans or transfer these sugar residues onto other glycans.”

    From Structure of the immunoregulatory sialidase NEU1 (2023) · cites this paper as [64]

    The Introduction’s “Maintenance of the modular classification and daily updates” section explains that GH denotes glycoside hydrolase families, but does not identify NEU1 or GH33. Searches for “NEU1 GH33” and “GH33 sialidase neuraminidase” found no passage in our copy establishing NEU1’s family assignment. (LLM, conf=0.76)

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Research works printed but not linked: 17

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Cited by

Sorted by citations

Authors
Drula, E., Garron, M.-L., Dogan, S., Lombard, V., Henrissat, B., & Terrapon, N.
Affiliations
  • Aix Marseille Univ, CNRS, UMR7257 AFMB, Marseille, France
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
Terrapon, Nicolas
Venue
Nucleic Acids Research
Published
2021-11-29
Volume
50
Issue
D1
Pages
D571-D577
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W3217216416
Cited by
2,439
References
2
Citations by year
2026: 552 · 2025: 576 · 2024: 606 · 2023: 473 · 2022: 229 · 2021: 1 · 2020: 1
FWCI
108.16
Type
journal article
Language
en
Open access
Locations
  • Nucleic Acids Research (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • HAL AMU (submittedVersion, other-oa)
  • HAL (submittedVersion)
  • Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion, cc-by-nc)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
Keywords
CAZy database, carbohydrate-active enzymes, enzyme annotation, Protein Data Bank structures
MeSH terms
Carbohydrates, Enzyme Activation, Enzymes, Humans, Databases, Nucleic Acid, Databases, Protein

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