The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A classification of glycosyl hydrolases based on amino acid sequence similarities
Open accessAbstract
The amino acid sequences of 301 glycosyl hydrolases and related enzymes have been compared. A total of 291 sequences corresponding to 39 EC entries could be classified into 35 families. Only ten sequences (less than 5% of the sample) could not be assigned to any family. With the sequences available for this analysis, 18 families were found to be monospecific (containing only one EC number) and 17 were found to be polyspecific (containing at least two EC numbers). Implications on the folding characteristics and mechanism of action of these enzymes and on the evolution of carbohydrate metabolism are discussed. With the steady increase in sequence and structural data, it is suggested that the enzyme classification system should perhaps be revised.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288
The relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
Cited by
Microbial Cellulose Utilization: Fundamentals and Biotechnology
Lynd, L. R., Weimer, P. J., van Zyl, W. H., & Pretorius, I. S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.3.506-577.2002 · Cited by 4,726
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
Henrissat, B., & Bairoch, A. (1993) · Biochemical Journal · doi:10.1042/bj2930781 · Cited by 1,974
Self-citationThe abundance and variety of carbohydrate-active enzymes in the human gut microbiota
Kaoutari, A. E., Armougom, F., Gordon, J. I., Raoult, D., & Henrissat, B. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro3050 · Cited by 1,683
Self-citationHenriksson, M., Henriksson, G., Berglund, L. A., & Lindström, T. (2007) · European Polymer Journal · doi:10.1016/j.eurpolymj.2007.05.038 · Cited by 1,183
Enzymatic conversion of lignocellulose into fermentable sugars: challenges and opportunities
Jørgensen, H., Kristensen, J. B., & Felby, C. (2007) · Biofuels, Bioproducts and Biorefining · doi:10.1002/bbb.4 · Cited by 1,143
Arabinoxylans and Endoxylanases in Wheat Flour Bread-making
Courtin, C. M., & Delcour, J. A. (2002) · Journal of Cereal Science · doi:10.1006/jcrs.2001.0433 · Cited by 720
Saponins and plant defence — a soap story
Osbourn, A. (1996) · Trends in Plant Science · doi:10.1016/s1360-1385(96)80016-1 · Cited by 382
Immune regulation by microbiome metabolites
Kim, C. H. (2018) · Immunology · doi:10.1111/imm.12930 · Cited by 375
Complex Carbohydrate Utilization by the Healthy Human Microbiome
Cantarel, B. L., Lombard, V., & Henrissat, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028742 · Cited by 378
Self-citationCharacterizing the mucin-degrading capacity of the human gut microbiota
Glover, J. S., Ticer, T. D., & Engevik, M. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-11819-z · Cited by 307
Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions
Langner, T., & Göhre, V. (2016) · Current Genetics · doi:10.1007/s00294-015-0530-x · Cited by 225
Fonzi, W. A. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.22.7070-7079.1999 · Cited by 193
Michel, G., Tonon, T., Scornet, D., Cock, J. M., & Kloareg, B. (2010) · New Phytologist · doi:10.1111/j.1469-8137.2010.03345.x · Cited by 188
Emerging Roles of β-Glucanases in Plant Development and Adaptative Responses
Perrot, T., Pauly, M., & Ramírez, V. (2022) · Plants · doi:10.3390/plants11091119 · Cited by 172
Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases
Vallée, F., Karaveg, K., Herscovics, A., Moremen, K. W., & Howell, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006927200 · Cited by 152
Burn, J. E., Hurley, U. A., Birch, R. J., Arioli, T., Cork, A., & Williamson, R. E. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.01483.x · Cited by 139
Biochemistry and molecular biology of exocellular fungal β-(1,3)- and β-(1,6)-glucanases
Martin, K., McDougall, B. M., McIlroy, S., Jayus, Chen, J., & Seviour, R. J. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00055.x · Cited by 127
Significance of chitinase-3-like protein 1 in the pathogenesis of inflammatory diseases and cancer
Yu, J. E., Yeo, I. J., Han, S.-B., Yun, J., Kim, B., Yong, Y. J., Lim, Y.-S., Kim, T. H., Son, D. J., & Hong, J. T. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01131-9 · Cited by 109
Bamford, N. C., Snarr, B. D., Gravelat, F. N., Little, D. J., Lee, M. J., Zacharias, C. A., Chabot, J. C., Geller, A. M., Baptista, S. D., Baker, P., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679050 · Cited by 102
Grevesse, C., Lepoivre, P., & Jijakli, M. H. (2003) · Phytopathology® · doi:10.1094/phyto.2003.93.9.1145 · Cited by 78
Treml, K., Meimaroglou, D., Hentges, A., & Bause, E. (2000) · Glycobiology · doi:10.1093/glycob/10.5.493 · Cited by 63
Arendt, C. W., & Ostergaard, H. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13117 · Cited by 55
Identification and enzymatic characterization of an endo-1,3-β-glucanase from Euglena gracilis
Takeda, T., Nakano, Y., Takahashi, M., Konno, N., Sakamoto, Y., Arashida, R., Marukawa, Y., Yoshida, E., Ishikawa, T., & Suzuki, K. (2015) · Phytochemistry · doi:10.1016/j.phytochem.2015.05.010 · Cited by 39
In situ extension as an approach for identifying novel α-amylase inhibitors.
Numao, S., Damager, I., Li, C., Wrodnigg, T. M., Begum, A., Overall, C. M., Brayer, G. D., & Withers, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406804200 · Cited by 24
Sumida, T., Hiraoka, S., Usui, K., Ishiwata, A., Sengoku, T., Stubbs, K. A., Tanaka, K., Deguchi, S., Fushinobu, S., & Nunoura, T. (2024) · Nature Communications · doi:10.1038/s41467-024-47653-2 · Cited by 13
Human Gut Metagenomes Encode Diverse GH156 Sialidases
Mann, E., Shekarriz, S., & Surette, M. G. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.01755-22 · Cited by 12
Predictions from Deep Learning Propose Substantial Protein-Carbohydrate Interplay
Canner, S. W., Schnaar, R. L., & Gray, J. J. (2025) · doi:10.1101/2025.03.07.641884 · Cited by 4
“For comparison, the total number of lectins identified by LectomeXplore is 230, or 1.1% of the UniProt reference proteome 22 , and the number known by CaZy is 349, or 1.7% 21 .”
InfluentialPredictions from deep learning propose substantial protein–carbohydrate interplay
Canner, S. W., Schnaar, R. L., & Gray, J. J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2523342123 · Cited by 4
Metadata
- Authors
- Henrissat, B.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1991-12-01
- Volume
- 280
- Issue
- 2
- Pages
- 309-316
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2113964973
- Cited by
- 3,188
- References
- 2
- FWCI
- 21.88
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
