GBA3

GBA3
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2E9L, 2E9M, 2JFE, 2ZOX, 3VKK
Identifiers
Aliases	GBA3, CBG, CBGL1, GLUC, KLRP, glucosylceramidase beta 3 (gene/pseudogene)
External IDs	OMIM: 606619; GeneCards: GBA3; OMA:GBA3 - orthologs
Gene location (Human)
Chr.	Chromosome 4 (human)
End	22,819,575 bp
RNA expression pattern
	Top expressed in
	jejunal mucosa; ; mucosa of ileum; ; duodenum; ; human kidney; ; liver; ; right lobe of liver; ; renal medulla; ; kidney tubule; ; buccal mucosa cell; ; testicle;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	beta-galactosidase activity; glycosylceramidase activity; hydrolase activity, hydrolyzing O-glycosyl compounds; beta-glucosidase activity; hydrolase activity; hydrolase activity, acting on glycosyl bonds; scopolin beta-glucosidase activity; glucosylceramidase activity; protein binding; galactosylceramidase activity;
Cellular component	cytoplasm; cytosol; catalytic complex;
Biological process	glycosylceramide catabolic process; metabolism; glycosphingolipid metabolic process; glycoside catabolic process; protein stabilization; cellular oligosaccharide catabolic process; positive regulation of exo-alpha-sialidase activity; carbohydrate metabolic process; glucosylceramide catabolic process; galactosylceramide catabolic process; beta-glucoside catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	57733
	n/a
	ENSG00000249948
	n/a
	Q9H227
	n/a
	NM_001128432; NM_001277225; NM_020973
	n/a
	NP_001121904; NP_001264154; NP_066024
	n/a
	Wikidata
View/Edit Human

Cytosolic beta-glucosidase, also known as cytosolic beta-glucosidase-like protein 1, is a beta-glucosidase (EC 3.2.1.21) enzyme that in humans is encoded by the GBA3 gene.^[3]^[4]

Function

Cytosolic beta-glucosidase is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides.^[4] GBA3 also has significant neutral glycosylceramidase activity (EC 3.2.1.62), suggesting that it may be involved in a non-lysosomal catabolic pathway of glucosylceramide metabolism.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000249948 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: glucosidase".
^ ^a ^b de Graaf M, van Veen IC, van der Meulen-Muileman IH, Gerritsen WR, Pinedo HM, Haisma HJ (June 2001). "Cloning and characterization of human liver cytosolic beta-glycosidase". Biochem. J. 356 (Pt 3): 907–10. doi:10.1042/0264-6021:3560907. PMC 1221920. PMID 11389701.
^ Hayashi Y, Okino N, Kakuta Y, Shikanai T, Tani M, Narimatsu H, Ito M (October 2007). "Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase". J. Biol. Chem. 282 (42): 30889–900. doi:10.1074/jbc.M700832200. PMID 17595169.

Bolmstedt A, Sjölander S, Hansen JE, Akerblom L, Hemming A, Hu SL, Morein B, Olofsson S (July 1996). "Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
Beutler E, Beutler L, West C (2004). "Mutations in the gene encoding cytosolic beta-glucosidase in Gaucher disease". J. Lab. Clin. Med. 144 (2): 65–8. doi:10.1016/j.lab.2004.03.013. PMID 15322500.
Yahata K, Mori K, Arai H, et al. (2000). "Molecular cloning and expression of a novel klotho-related protein". J. Mol. Med. 78 (7): 389–94. doi:10.1007/s001090000131. PMID 11043382. S2CID 20851692.
Pantophlet R, Wilson IA, Burton DR (2003). "Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design". J. Virol. 77 (10): 5889–901. doi:10.1128/JVI.77.10.5889-5901.2003. PMC 154011. PMID 12719582.
Tribolo S, Berrin JG, Kroon PA, et al. (2007). "The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase". J. Mol. Biol. 370 (5): 964–75. doi:10.1016/j.jmb.2007.05.034. PMID 17555766.
Noguchi J, Hayashi Y, Baba Y, et al. (2008). "Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase". Biochem. Biophys. Res. Commun. 374 (3): 549–52. doi:10.1016/j.bbrc.2008.07.089. PMID 18662675.
Berrin JG, Czjzek M, Kroon PA, et al. (2003). "Substrate (aglycone) specificity of human cytosolic beta-glucosidase". Biochem. J. 373 (Pt 1): 41–8. doi:10.1042/BJ20021876. PMC 1223474. PMID 12667141.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Wolk T, Schreiber M (2006). "N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization". Med. Microbiol. Immunol. 195 (3): 165–72. doi:10.1007/s00430-006-0016-z. PMID 16547752. S2CID 31347157.
Papandreou MJ, Fenouillet E (1997). "Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation". FEBS Lett. 406 (1–2): 191–5. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416. S2CID 17660.
Dekker N, Voorn-Brouwer T, Verhoek M, et al. (2010). "The cytosolic beta-glucosidase GBA3 does not influence type 1 Gaucher disease manifestation". Blood Cells Mol. Dis. 46 (1): 19–26. doi:10.1016/j.bcmd.2010.07.009. PMID 20728381.
Berrin JG, McLauchlan WR, Needs P, et al. (2002). "Functional expression of human liver cytosolic beta-glucosidase in Pichia pastoris. Insights into its role in the metabolism of dietary glucosides". Eur. J. Biochem. 269 (1): 249–58. doi:10.1046/j.0014-2956.2001.02641.x. PMID 11784319.
Feizi T, Larkin M (1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID 2136376.
Németh K, Plumb GW, Berrin JG, et al. (2003). "Deglycosylation by small intestinal epithelial cell beta-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans". Eur J Nutr. 42 (1): 29–42. doi:10.1007/s00394-003-0397-3. PMID 12594539. S2CID 20146480.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. hdl:1874/5091. PMID 11530211. S2CID 13576808.
Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin". J. Gen. Virol. 84 (Pt 2): 353–60. doi:10.1099/vir.0.18734-0. PMID 12560567.

External links

PDBe-KB provides an overview of all the structure information available in the PDB for Human Cytosolic beta-glucosidase

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000249948 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-3] "Entrez Gene: glucosidase".

[pmid11389701-4] Graaf M, van Veen IC, van der Meulen-Muileman IH, Gerritsen WR, Pinedo HM, Haisma HJ (June 2001). "Cloning and characterization of human liver cytosolic beta-glycosidase". Biochem. J. 356 (Pt 3): 907–10. doi:10.1042/0264-6021:3560907. PMC 1221920. PMID 11389701.

[pmid17595169-5] Hayashi Y, Okino N, Kakuta Y, Shikanai T, Tani M, Narimatsu H, Ito M (October 2007). "Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase". J. Biol. Chem. 282 (42): 30889–900. doi:10.1074/jbc.M700832200. PMID 17595169.

[1]

[2]

[3]

[4]

[5]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

GBA3

Function

See also

References

Further reading

External links