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Galactosidase
From Proteopedia
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{{STRUCTURE_3e1f| PDB=3e1f | SIZE=400| SCENE=Galactosidase/Cv/1 |right|CAPTION=E. coli β-galactosidase tetramer complex with β-D-galactose, DMSO, Mg+2 and Na+ ions, [[3e1f]] }} | {{STRUCTURE_3e1f| PDB=3e1f | SIZE=400| SCENE=Galactosidase/Cv/1 |right|CAPTION=E. coli β-galactosidase tetramer complex with β-D-galactose, DMSO, Mg+2 and Na+ ions, [[3e1f]] }} | ||
| + | == Function == | ||
| - | '''α-Galactosidase''' (Agal) hydrolyzes the terminal α-galactosyl moiety from glycoproteins and glycolipids. '''β-Galactosidase''' (Bgal) hydrolyzes β-galactosides into monosaccharides. | + | '''α-Galactosidase''' (Agal) hydrolyzes the terminal α-galactosyl moiety from glycoproteins and glycolipids<ref>PMID:15003450</ref>. '''β-Galactosidase''' (Bgal) hydrolyzes β-galactosides into monosaccharides<ref>PMID:8008071</ref>. |
Isopropyl-β-d-thiogalactopyranoside (IPTG) induces Bgal activity. Phenylethyl-β-d-thiogalactopyranoside (PETG) is an inhibitor. Galactose, lactose, o-nitrophenyl-β-d-galactoside (ONPG) are substrates. Galactopyranosyl is reaction intermediate. For details on β-galactosidase see [[Molecular Playground/Beta-galactosidase]]. | Isopropyl-β-d-thiogalactopyranoside (IPTG) induces Bgal activity. Phenylethyl-β-d-thiogalactopyranoside (PETG) is an inhibitor. Galactose, lactose, o-nitrophenyl-β-d-galactoside (ONPG) are substrates. Galactopyranosyl is reaction intermediate. For details on β-galactosidase see [[Molecular Playground/Beta-galactosidase]]. | ||
| + | |||
| + | == Disease == | ||
| + | |||
| + | The inherited deficiency of Agal is the cause of Fabry disease<ref>PMID:5411915</ref>. Bgal deficiency can lead to galactosialidosis<ref>PMID:1683129</ref>. | ||
== 3D Structures of Galactosidase == | == 3D Structures of Galactosidase == | ||
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**[[2v4v]] – gal GH59 – ''Clostridium cellulolyticum'' | **[[2v4v]] – gal GH59 – ''Clostridium cellulolyticum'' | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
<br /> | <br /> | ||
*Created with the participation of [[User:Wayne Decatur|Wayne Decatur]]. | *Created with the participation of [[User:Wayne Decatur|Wayne Decatur]]. | ||
Revision as of 10:11, 3 March 2016
Contents |
Function
α-Galactosidase (Agal) hydrolyzes the terminal α-galactosyl moiety from glycoproteins and glycolipids[1]. β-Galactosidase (Bgal) hydrolyzes β-galactosides into monosaccharides[2]. Isopropyl-β-d-thiogalactopyranoside (IPTG) induces Bgal activity. Phenylethyl-β-d-thiogalactopyranoside (PETG) is an inhibitor. Galactose, lactose, o-nitrophenyl-β-d-galactoside (ONPG) are substrates. Galactopyranosyl is reaction intermediate. For details on β-galactosidase see Molecular Playground/Beta-galactosidase.
Disease
The inherited deficiency of Agal is the cause of Fabry disease[3]. Bgal deficiency can lead to galactosialidosis[4].
3D Structures of Galactosidase
Updated on 03-March-2016
For 3hg2 .
References
- ↑ Garman SC, Garboczi DN. The molecular defect leading to Fabry disease: structure of human alpha-galactosidase. J Mol Biol. 2004 Mar 19;337(2):319-35. PMID:15003450 doi:10.1016/j.jmb.2004.01.035
- ↑ Jacobson RH, Zhang XJ, DuBose RF, Matthews BW. Three-dimensional structure of beta-galactosidase from E. coli. Nature. 1994 Jun 30;369(6483):761-6. PMID:8008071 doi:http://dx.doi.org/10.1038/369761a08015589
- ↑ Kint JA. Fabry's disease: alpha-galactosidase deficiency. Science. 1970 Feb 27;167(3922):1268-9. PMID:5411915
- ↑ Weil-Hillman G, Levi R, Zakay-Rones Z. Increase in concanavalin A cap formation on lymphoma cells following interaction with inactive influenza viruses. Acta Virol. 1991 May;35(3):238-46. PMID:1683129
- Created with the participation of Wayne Decatur.
