3.2.1.- Glycosidases

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3.2.1.- Glycosidases

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

Enzymes

amylase alpha 2A Show summary »« Hide summary More detailed page go icon to follow link

alpha glucosidase Show summary »« Hide summary More detailed page go icon to follow link

Target Id

2611

Nomenclature

alpha glucosidase

Previous and unofficial names

glucosidase | glucosidase, alpha, acid | glucosidase, alpha; acid | glucosidase alpha, acid | lysosomal alpha-glucosidase

Genes

GAA (Hs), Gaa (Mm), Gaa (Rn)

Ensembl ID

ENSG00000171298 (Hs), ENSMUSG00000025579 (Mm), ENSRNOG00000047656 (Rn)

UniProtKB AC

P10253 (Hs), P70699 (Mm), Q6P7A9 (Rn)

EC number

3.2.1.20

glucosylceramidase beta C Show summary »« Hide summary More detailed page go icon to follow link

Target Id

2978

Nomenclature

glucosylceramidase beta

Previous and unofficial names

Genes

GBA1 (Hs), Gba (Mm), Gba (Rn)

Ensembl ID

ENSG00000177628 (Hs), ENSMUSG00000028048 (Mm), ENSRNOG00000049281 (Rn)

UniProtKB AC

P04062 (Hs), P17439 (Mm)

EC number

3.2.1.21
Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose.

3.2.1.45
D-glucosyl-N-acylsphingosine + H₂O <=> D-glucose + N-acylsphingosine

Comment

The GBA protein is an enzyme that cleaves the beta-glucosidic linkage of glycosylceramide. Mutations in the GBA gene that inactivate the enzymatic function of GBA cause the lysosomal storage disorder, Gaucher's disease, and are a genetic risk factor for developing Parkinson's disease [1,3].

maltase-glucoamylase Show summary »« Hide summary More detailed page go icon to follow link

Target Id

2627

Nomenclature

maltase-glucoamylase

Previous and unofficial names

maltase-glucoamylase, intestinal | MGA | maltase-glucoamylase (alpha-glucosidase)

Genes

MGAM (Hs), Mgam (Mm), Mgam (Rn)

Ensembl ID

ENSG00000257335 (Hs), ENSMUSG00000068587 (Mm)

UniProtKB AC

O43451 (Hs)

EC number

3.2.1.20

3.2.1.3

Inhibitors

miglitol pK_i 6.0 [2]

heparanase Show summary »« Hide summary More detailed page go icon to follow link

Target Id

2996

Nomenclature

heparanase

Previous and unofficial names

HPA | HPSE1 | HSE1

Genes

HPSE (Hs), Hpse (Mm), Hpse (Rn)

Ensembl ID

ENSG00000173083 (Hs), ENSMUSG00000035273 (Mm), ENSRNOG00000002188 (Rn)

UniProtKB AC

Q9Y251 (Hs)

EC number

3.2.1.166
Cleavage of heparan sulfate glycosaminoglycans from proteoglycan core proteins and degradation of these to small oligosaccharides. Endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan

klotho Show summary »« Hide summary More detailed page go icon to follow link

Germain DP, Puech JP, Caillaud C, Kahn A, Poenaru L. (1998) Exhaustive screening of the acid beta-glucosidase gene, by fluorescence-assisted mismatch analysis using universal primers: mutation profile and genotype/phenotype correlations in Gaucher disease. Am J Hum Genet, 63 (2): 415-27. [PMID:9683600]

Gómez G, Arias S, Cárdenas L, Zoghbi D, Paradisi I. (2017) GBA mutations in Gaucher type I Venezuelan patients: ethnic origins and frequencies. J Genet, 96 (4): 583-589. [PMID:28947706]

* Robak LA, Jansen IE, van Rooij J, Uitterlinden AG, Kraaij R, Jankovic J, International Parkinson’s Disease Genomics Consortium (IPDGC), Heutink P, Shulman JM, IPDGC Consortium members et al.. (2017) Excessive burden of lysosomal storage disorder gene variants in Parkinson's disease. Brain, 140 (12): 3191-3203. [PMID:29140481]

* Schneider SA, Alcalay RN. (2017) Neuropathology of genetic synucleinopathies with parkinsonism: Review of the literature. Mov Disord, 32 (11): 1504-1523. [PMID:29124790]

Yilmazer B, Yagci ZB, Bakar E, Ozden B, Ulgen K, Ozkirimli E. (2017) Investigation of novel pharmacological chaperones for Gaucher Disease. J Mol Graph Model, 76: 364-378. [PMID:28763689]

References

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1. Beavan MS, Schapira AH. (2013) Glucocerebrosidase mutations and the pathogenesis of Parkinson disease. Ann Med, 45 (8): 511-21. [PMID:24219755]

2. Mohan S, Sim L, Rose DR, Pinto BM. (2010) Probing the active-site requirements of human intestinal N-terminal maltase-glucoamylase: Synthesis and enzyme inhibitory activities of a six-membered ring nitrogen analogue of kotalanol and its de-O-sulfonated derivative. Bioorg Med Chem, 18 (22): 7794-8. [PMID:20970346]

3. Robak LA, Jansen IE, van Rooij J, Uitterlinden AG, Kraaij R, Jankovic J, International Parkinson’s Disease Genomics Consortium (IPDGC), Heutink P, Shulman JM, IPDGC Consortium members et al.. (2017) Excessive burden of lysosomal storage disorder gene variants in Parkinson's disease. Brain, 140 (12): 3191-3203. [PMID:29140481]

How to cite this family page

Database page citation:

3.2.1.- Glycosidases. Accessed on 04/12/2022. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=841.

Concise Guide to PHARMACOLOGY citation:

Alexander SP, Fabbro D, Kelly E, Mathie A, Peters JA, Veale EL et al. (2021) THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Enzymes. Br J Pharmacol. 178 Suppl 1:S313-S411.