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InterPro: IPR000514 Glycoside hydrolase, family 39
Protein matches
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UniProtKB Matches: 160 proteins |
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Accession
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IPR000514 Glyco_hydro_39 |
Type
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Family |
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:0005975 carbohydrate metabolic process
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Function
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GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
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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 39 GH39 comprises enzymes with several known activities; alpha-L-iduronidase (EC:3.2.1.76); beta-xylosidase (EC:3.2.1.37).
The most highly conserved regions in these enzymes are located in their N-terminal
sections. These contain a glutamic acid residue which, on the basis of
similarities with other families of glycosyl hydrolases [1], probably acts as
the proton donor in their catalytic mechanism.
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Structural links
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Database links
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Pfam Clan: CL0058.12
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Additional Reading
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Czjzek M, Bravman T, Henrissat B, Shoham Y.
Crystallization and preliminary X-ray analysis of family 39 beta-D-xylosidase from Geobacillus stearothermophilus T-6.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 583-5
[PubMed: 14993701]
http://dx.doi.org/10.1107/S0907444904001088
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Yang JK, Yoon HJ, Ahn HJ, Lee BI, Pedelacq JD, Liong EC, Berendzen J, Laivenieks M, Vieille C, Zeikus GJ, Vocadlo DJ, Withers SG, Suh SW.
Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase.
J. Mol. Biol. 335 2004 155-65
[PubMed: 14659747]
http://dx.doi.org/10.1016/j.jmb.2003.10.026
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Stoltzfus LJ, Sosa-Pineda B, Moskowitz SM, Menon KP, Dlott B, Hooper L, Teplow DB, Shull RM, Neufeld EF.
Cloning and characterization of cDNA encoding canine alpha-L-iduronidase. mRNA deficiency in mucopolysaccharidosis I dog.
J. Biol. Chem. 267 1992 6570-5
[PubMed: 1551868]
http://intl.jbc.org/cgi/reprint/267/10/6570.pdf
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Henrissat B, Bairoch A.
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 293 ( Pt 3) 1993 781-8
[PubMed: 8352747]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8352747&action=stream&blobtype=pdf
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Czjzek M, Ben David A, Bravman T, Shoham G, Henrissat B, Shoham Y.
Enzyme-substrate complex structures of a GH39 beta-xylosidase from Geobacillus stearothermophilus.
J. Mol. Biol. 353 2005 838-46
[PubMed: 16212978]
http://dx.doi.org/10.1016/j.jmb.2005.09.003
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InterPro 23.1
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