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InterPro: IPR001661 Glycoside hydrolase, family 37
Protein matches
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UniProtKB Matches: 681 proteins |
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Accession
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IPR001661 Glyco_hydro_37 |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR008928 Six-hairpin glycosidase-like
IPR018232 Glycoside hydrolase, family 37, conserved site
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GO Term annotation
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Process
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GO:0005991 trehalose metabolic process
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Function
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GO:0004555 alpha,alpha-trehalase activity
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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 37 GH37
comprises enzymes with only one known activity; trehalase (EC:3.2.1.28).
Trehalase is the enzyme responsible for the degradation of the disaccharide alpha,alpha-trehalose yielding two glucose subunits [5]. It is an enzyme found in a wide variety of organisms and whose sequence has been highly conserved throughout evolution.
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Structural links
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Database links
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Pfam Clan: CL0211.5
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Additional Reading
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Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, Garcia A, Chiara JL, Davies GJ.
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors.
Angew. Chem. Int. Ed. Engl. 46 2007 4115-9
[PubMed: 17455176]
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Voit EO.
Biochemical and genomic regulation of the trehalose cycle in yeast: review of observations and canonical model analysis.
J. Theor. Biol. 223 2003 55-78
[PubMed: 12782117]
http://dx.doi.org/10.1016/S0022-5193(03)00072-9
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InterPro 23.1
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