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InterPro: IPR001139 Glycoside hydrolase, family 30
Protein matches
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UniProtKB Matches: 425 proteins |
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Accession
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IPR001139 Glyco_hydro_30 |
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Type
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Family |
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Signatures
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InterPro Relationships
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Contains
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IPR013781 Glycoside hydrolase, subgroup, catalytic core
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GO Term annotation
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Process
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GO:0006665 sphingolipid metabolic process
GO:0007040 lysosome organization
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Function
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GO:0004348 glucosylceramidase activity
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Component
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GO:0005764 lysosome
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Glycoside hydrolase family 30 GH30
comprises enzymes with only one known activity; glucosylceramidase (EC:3.2.1.45).
Family 30 encompasses the mammalian glucosylceramidases. Human acid beta-glucosidase (D-glucosyl-N-acylsphingosine glucohydrolase),
cleaves the glucosidic bonds of glucosylceramide and synthetic beta-glucosides [5]. Any one of over 50 different mutations in the gene of glucocerebrosidase have been found to affect activity of this hydrolase, producing variants of Gaucher disease, the most prevalent lysosomal storage disease [5, 6].
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Structural links
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Database links
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Pfam Clan: CL0058.12
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Publications
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1.
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Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995
[PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
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2.
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Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995
[PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
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3.
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Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
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4.
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Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
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5.
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Dinur T, Osiecki KM, Legler G, Gatt S, Desnick RJ, Grabowski GA.
Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site.
Proc. Natl. Acad. Sci. U.S.A. 83 1660-4 1986
[PubMed: 3456607]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=3456607
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6.
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Iwasawa K, Ida H, Eto Y.
Differences in origin of the 1448C mutation in patients with Gaucher disease.
39 451-3 1997
[PubMed: 9316290]
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Additional Reading
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Lieberman RL, Wustman BA, Huertas P, Powe AC Jr, Pine CW, Khanna R, Schlossmacher MG, Ringe D, Petsko GA.
Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease.
Nat. Chem. Biol. 3 2007 101-7
[PubMed: 17187079]
http://dx.doi.org/10.1038/nchembio850
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Shaaltiel Y, Bartfeld D, Hashmueli S, Baum G, Brill-Almon E, Galili G, Dym O, Boldin-Adamsky SA, Silman I, Sussman JL, Futerman AH, Aviezer D.
Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system.
Plant Biotechnol. J. 5 2007 579-90
[PubMed: 17524049]
http://dx.doi.org/10.1111/j.1467-7652.2007.00263.x
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Brumshtein B, Wormald MR, Silman I, Futerman AH, Sussman JL.
Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease.
Acta Crystallogr. D Biol. Crystallogr. 62 2006 1458-65
[PubMed: 17139081]
http://dx.doi.org/10.1107/S0907444906038303
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Beutler E.
Gaucher disease phenotypes outflanked?
Genome Res. 7 1997 950-1
[PubMed: 9331364]
http://www.genome.org/cgi/content/abstract/7/10/950
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Liou B, Kazimierczuk A, Zhang M, Scott CR, Hegde RS, Grabowski GA.
Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations.
J. Biol. Chem. 281 2006 4242-53
[PubMed: 16293621]
http://dx.doi.org/10.1074/jbc.M511110200
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Brumshtein B, Greenblatt HM, Butters TD, Shaaltiel Y, Aviezer D, Silman I, Futerman AH, Sussman JL.
Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher disease.
J. Biol. Chem. 282 2007 29052-8
[PubMed: 17666401]
http://dx.doi.org/10.1074/jbc.M705005200
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Winfield SL, Tayebi N, Martin BM, Ginns EI, Sidransky E.
Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease.
Genome Res. 7 1997 1020-6
[PubMed: 9331372]
http://www.genome.org/cgi/content/abstract/7/10/1020
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el Hassouni M, Henrissat B, Chippaux M, Barras F.
Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans.
J. Bacteriol. 174 1992 765-77
[PubMed: 1732212]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1732212&action=stream&blobtype=pdf
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InterPro 23.1
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