New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
Open accessAbstract
301 glycosyl hydrolases and related enzymes corresponding to 39 EC entries of the I.U.B. classification system have been classified into 35 families on the basis of amino-acid-sequence similarities [Henrissat (1991) Biochem. J. 280, 309-316]. Approximately half of the families were found to be monospecific (containing only one EC number), whereas the other half were found to be polyspecific (containing at least two EC numbers). A > 60% increase in sequence data for glycosyl hydrolases (181 additional enzymes or enzyme domains sequences have since become available) allowed us to update the classification not only by the addition of more members to already identified families, but also by the finding of ten new families. On the basis of a comparison of 482 sequences corresponding to 52 EC entries, 45 families, out of which 22 are polyspecific, can now be defined. This classification has been implemented in the SWISS-PROT protein sequence data bank.
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The α-subunit of α-glucosidase II contains a GH31 consensus sequence domain (G/F)-(L/I/V/M)-W-X-D-M-N-E providing a nucleophile retaining enzyme mechanism.
“The α-subunit contains a GH31 consensus sequence domain (G/F)-(L/I/V/M)-W-X-D-M-N-E providing a nucleophile retaining enzyme mechanism [365,366].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [366]
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“The α-subunit contains a GH31 consensus sequence domain (G/F)-(L/I/V/M)-W-X-D-M-N-E providing a nucleophile retaining enzyme mechanism [365,366].”
Background
- Authors
- Henrissat, B., & Bairoch, A.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of Geneva (CH)
- Corresponding author
- Henrissat, B
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1993-08-01
- Volume
- 293
- Issue
- 3
- Pages
- 781-788
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1134435
- OpenAlex
- W1772341111
- Cited by
- 1,974
- References
- 0
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 22 · 2023: 24 · 2022: 37 · 2021: 34 · 2020: 37 · 2019: 44 · 2018: 40 · 2017: 36 · 2016: 42 · 2015: 50 · 2014: 52 · 2013: 67 · 2012: 67
- FWCI
- 51.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- glycoside hydrolases, enzyme family classification, amino acid sequence similarity, EC numbers, enzyme domains, Swiss-Prot, carbohydrate-active enzymes
- MeSH terms
- Glycoside Hydrolases, Sequence Homology, Amino Acid
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