{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T07:17:20Z","timestamp":1761895040656,"version":"3.37.3"},"reference-count":28,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2024,5,10]],"date-time":"2024-05-10T00:00:00Z","timestamp":1715299200000},"content-version":"vor","delay-in-days":5274,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-sa\/3.0\/"}],"funder":[{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["DBI-0354771","ITR-IIS-0407204","DBI-0542119","CCF0621700"],"award-info":[{"award-number":["DBI-0354771","ITR-IIS-0407204","DBI-0542119","CCF0621700"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Cellulases are important glycosyl hydrolases (GHs) that hydrolyze cellulose polymers into smaller oligosaccharides by breaking the cellulose \u03b2 (1\u21924) bonds, and they are widely used to produce cellulosic ethanol from the plant biomass. N-linked and O-linked glycosylations were proposed to impact the catalytic efficiency, cellulose binding affinity and the stability of cellulases based on observations of individual cellulases. As far as we know, there has not been any systematic analysis of the distributions of N-linked and O-linked glycosylated residues in cellulases, mainly due to the limited annotations of the relevant functional domains and the glycosylated residues. We have computationally annotated the functional domains and glycosylated residues in cellulases, and conducted a systematic analysis of the distributions of the N-linked and O-linked glycosylated residues in these enzymes. Many N-linked glycosylated residues were known to be in the GH domains of cellulases, but they are there probably just by chance, since the GH domain usually occupies more than half of the sequence length of a cellulase. Our analysis indicates that the O-linked glycosylated residues are significantly enriched in the linker regions between the carbohydrate binding module (CBM) domains and GH domains of cellulases. Possible mechanisms are discussed.<\/jats:p>","DOI":"10.1016\/s1672-0229(08)60049-2","type":"journal-article","created":{"date-parts":[[2010,2,20]],"date-time":"2010-02-20T09:48:32Z","timestamp":1266659312000},"page":"194-199","source":"Crossref","is-referenced-by-count":27,"title":["Large-Scale Analyses of Glycosylation in Cellulases"],"prefix":"10.1093","volume":"7","author":[{"given":"Fengfeng","family":"Zhou","sequence":"first","affiliation":[{"name":"Computational Systems Biology Laboratory, Department of Biochemistry and Molecular Biology \/ Institute of Bioinformatics, University of Georgia , Athens, GA, 30602-7229 , USA"},{"name":"BioEnergy Science Center, Oak Ridge National Laboratory , Oak Ridge, TN, 37830-8050 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Victor","family":"Olman","sequence":"additional","affiliation":[{"name":"Computational Systems Biology Laboratory, Department of Biochemistry and Molecular Biology \/ Institute of Bioinformatics, University of Georgia , Athens, GA, 30602-7229 , USA"},{"name":"BioEnergy Science Center, Oak Ridge National Laboratory , Oak Ridge, TN, 37830-8050 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ying","family":"Xu","sequence":"additional","affiliation":[{"name":"Computational Systems Biology Laboratory, Department of Biochemistry and Molecular Biology \/ Institute of Bioinformatics, University of Georgia , Athens, GA, 30602-7229 , USA"},{"name":"BioEnergy Science Center, Oak Ridge National Laboratory , Oak Ridge, TN, 37830-8050 , USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2010,2,19]]},"reference":[{"key":"2024051008263285900_bib1","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1128\/MMBR.66.3.506-577.2002","article-title":"Microbial cellulose utilization: fundamentals and biotechnology","volume":"66","author":"Lynd","year":"2002","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"2024051008263285900_bib2","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.pbi.2008.03.003","article-title":"Wood cell walls: biosynthesis, developmental dynamics and their implications for wood properties","volume":"11","author":"Mellerowicz","year":"2008","journal-title":"Curr. Opin. Plant Biol."},{"key":"2024051008263285900_bib3","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.1111\/j.1432-1033.2004.04031.x","article-title":"Heterogeneity of homologously expressed Hypocrea jecorina (Trichoderma reesei) Cel7B catalytic module","volume":"271","author":"Eriksson","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"2024051008263285900_bib4","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/S0141-0229(99)00035-6","article-title":"Cellulase production by Neurospora crassa on wheat straw","volume":"25","author":"Romero","year":"1999","journal-title":"Enzyme Microb. Technol."},{"key":"2024051008263285900_bib5","doi-asserted-by":"crossref","first-page":"201","DOI":"10.3109\/10409239609106584","article-title":"The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation","volume":"31","author":"B\u00e9guin","year":"1996","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"2024051008263285900_bib6","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0065-2911(08)60015-6","article-title":"Physiology of carbohydrate to solvent conversion by clostridia","volume":"39","author":"Mitchell","year":"1998","journal-title":"Adv. Microb. Physiol."},{"key":"2024051008263285900_bib7","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1094\/MPMI-19-1072","article-title":"Microbial endoxylanases: effective weapons to breach the plant cell-wall barrier or, rather, triggers of plant defense systems?","volume":"19","author":"Beli\u00ebn","year":"2006","journal-title":"Mol. Plant Microbe Interact."},{"key":"2024051008263285900_bib8","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3109\/07388559709146606","article-title":"Xylanolytic enzymes from fungi and bacteria","volume":"17","author":"Sunna","year":"1997","journal-title":"Crit. Rev. Biotechnol."},{"key":"2024051008263285900_bib9","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0167-7012(02)00028-3","article-title":"Measurement and characterization of cellulase activity in sclerophyllous forest litter","volume":"50","author":"Criquet","year":"2002","journal-title":"J. Microbiol. Methods"},{"key":"2024051008263285900_bib10","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.copbio.2008.04.007","article-title":"Extremely thermophilic microorganisms for biomass conversion: status and prospects","volume":"19","author":"Blumer-Schuette","year":"2008","journal-title":"Curr. Opin. Biotechnol."},{"key":"2024051008263285900_bib11","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1111\/j.1365-2958.2007.05640.x","article-title":"Cellulosomes: microbial nanomachines that display plasticity in quaternary structure","volume":"63","author":"Gilbert","year":"2007","journal-title":"Mol. Microbiol."},{"key":"2024051008263285900_bib12","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.copbio.2008.04.008","article-title":"A biophysical perspective on the cellulosome: new opportunities for biomass conversion","volume":"19","author":"Ding","year":"2008","journal-title":"Curr. Opin. Biotechnol."},{"key":"2024051008263285900_bib13","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1186\/1471-2105-8-438","article-title":"Glycosylation site prediction using ensembles of support vector machine classifiers.","volume":"8","author":"Caragea","year":"2007","journal-title":"BMC Bioinformatics"},{"key":"2024051008263285900_bib14","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/S1367-5931(99)00021-6","article-title":"Effect of N-linked glycosylation on glycopeptide and glycoprotein structure","volume":"3","author":"Imperiali","year":"1999","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2024051008263285900_bib15","doi-asserted-by":"crossref","first-page":"8421","DOI":"10.1021\/ja0496266","article-title":"Effects of glycosylation on peptide conformation: a synergistic experimental and computational study","volume":"126","author":"Bosques","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"2024051008263285900_bib16","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1046\/j.1432-1327.1998.2560119.x","article-title":"Modified glycosylation of cellobiohydrolase I from a high cellulase-producing mutant strain of Trichoderma reesei","volume":"256","author":"Harrison","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"2024051008263285900_bib17","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/1754-6834-1-10","article-title":"Implications of cellobiohydrolase glycosylation for use in biomass conversion","volume":"1","author":"Jeoh","year":"2008","journal-title":"Biotechnol. Biofuels"},{"key":"2024051008263285900_bib18","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0378-1119(92)90173-M","article-title":"Streptomyces lividans glycosylates an exoglucanase (Cex) from Cellulomonas fimi","volume":"121","author":"MacLeod","year":"1992","journal-title":"Gene"},{"key":"2024051008263285900_bib19","first-page":"89","article-title":"UniProtKB\/Swiss-Prot","volume":"406","author":"Boutet","year":"2007","journal-title":"Methods Mol. Biol."},{"key":"2024051008263285900_bib20","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1007\/978-1-59745-515-2_4","article-title":"Pfam: a domain-centric method for analyzing proteins and proteomes","volume":"396","author":"Mistry","year":"2007","journal-title":"Methods Mol. Biol."},{"key":"2024051008263285900_bib21","doi-asserted-by":"crossref","first-page":"7695","DOI":"10.1073\/pnas.0902340106","article-title":"A transcriptomic analysis of superhybrid rice LYP9 and its parents","volume":"106","author":"Wei","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2024051008263285900_bib22","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/S1672-0229(08)60025-X","article-title":"Hidden Markov models incorporating fuzzy measures and integrals for protein sequence identification and alignment","volume":"6","author":"Bidargaddi","year":"2008","journal-title":"Genomics Proteomics Bioinformatics"},{"key":"2024051008263285900_bib23","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S1672-0229(07)60001-1","article-title":"Comparative analysis of eubacterial DNA polymerase III alpha subunits","volume":"4","author":"Zhao","year":"2006","journal-title":"Genomics Proteomics Bioinformatics"},{"key":"2024051008263285900_bib24","doi-asserted-by":"crossref","first-page":"D187","DOI":"10.1093\/nar\/gkj161","article-title":"The Universal Protein Resource (UniProt): an expanding universe of protein information","volume":"34","author":"Wu","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"2024051008263285900_bib25","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.copbio.2008.05.003","article-title":"Importance of systems biology in engineering microbes for biofuel production","volume":"19","author":"Mukhopadhyay","year":"2008","journal-title":"Curr. Opin. Biotechnol."},{"key":"2024051008263285900_bib26","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1093\/nar\/28.1.304","article-title":"The ENZYME database in 2000","volume":"28","author":"Bairoch","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"2024051008263285900_bib27","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.jmb.2004.05.028","article-title":"Improved prediction of signal peptides: SignalP 3.0","volume":"340","author":"Bendtsen","year":"2004","journal-title":"J. Mol. Biol."},{"key":"2024051008263285900_bib28","doi-asserted-by":"crossref","first-page":"D247","DOI":"10.1093\/nar\/gkj149","article-title":"Pfam: clans, web tools and services","volume":"34","author":"Finn","year":"2006","journal-title":"Nucleic Acids Res."}],"container-title":["Genomics, Proteomics &amp; Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1672022908600492?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1672022908600492?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/academic.oup.com\/gpb\/article-pdf\/7\/4\/194\/57483101\/gpb_7_4_194.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/gpb\/article-pdf\/7\/4\/194\/57483101\/gpb_7_4_194.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,10]],"date-time":"2024-05-10T08:28:20Z","timestamp":1715329700000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/gpb\/article\/7\/4\/194\/7221814"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,12,1]]},"references-count":28,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2009,12,1]]}},"URL":"https:\/\/doi.org\/10.1016\/s1672-0229(08)60049-2","relation":{},"ISSN":["1672-0229","2210-3244"],"issn-type":[{"type":"print","value":"1672-0229"},{"type":"electronic","value":"2210-3244"}],"subject":[],"published-other":{"date-parts":[[2009,12]]},"published":{"date-parts":[[2009,12,1]]}}}