Biology:ALG6

Generic protein structure example

Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase is an enzyme that in humans is encoded by the ALG6 gene.

Function

This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic.

Further reading

• "A novel carbohydrate-deficient glycoprotein syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharide". The Journal of Clinical Investigation 102 (4): 647–52. Aug 1998. doi:10.1172/JCI2266. PMID 9710431. 
• "Carbohydrate-deficient glycoprotein syndrome type V: deficiency of dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase". Proceedings of the National Academy of Sciences of the United States of America 95 (22): 13200–5. Oct 1998. doi:10.1073/pnas.95.22.13200. PMID 9789065. PMC 23759. Bibcode: 1998PNAS...9513200K. http://goedoc.uni-goettingen.de/goescholar/bitstream/handle/1/3444/319.%20Carbohydrate-deficient%20glycoprotein%20syndrome%20type%20V%20....pdf?sequence=1. 
• "Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic". Human Genetics 106 (5): 538–45. May 2000. doi:10.1007/s004390050022. PMID 10914684. 
• "Analysis of multiple mutations in the hALG6 gene in a patient with congenital disorder of glycosylation Ic". Molecular Genetics and Metabolism 70 (3): 219–23. Jul 2000. doi:10.1006/mgme.2000.3017. PMID 10924277. 
• "Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation". The American Journal of Pathology 157 (6): 1917–25. Dec 2000. doi:10.1016/S0002-9440(10)64830-4. PMID 11106564. 
• "A broad spectrum of clinical presentations in congenital disorders of glycosylation I: a series of 26 cases". Journal of Medical Genetics 38 (1): 14–9. Jan 2001. doi:10.1136/jmg.38.1.14. PMID 11134235. 
• "The T911C (F304S) substitution in the human ALG6 gene is a common polymorphism and not a causal mutation of CDG-Ic". Journal of Human Genetics 46 (9): 547–8. 2001. doi:10.1007/s100380170038. PMID 11558905. 
• "Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate". Molecular Biology and Evolution 19 (9): 1451–63. Sep 2002. doi:10.1093/oxfordjournals.molbev.a004208. PMID 12200473. 
• "DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG)". European Journal of Human Genetics 10 (10): 643–8. Oct 2002. doi:10.1038/sj.ejhg.5200858. PMID 12357336. 
• "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Experimental Cell Research 288 (1): 35–50. Aug 2003. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157. 
• "Identification of a frequent variant in ALG6, the cause of Congenital Disorder of Glycosylation-Ic". Human Mutation 22 (5): 420–1. Nov 2003. doi:10.1002/humu.9195. PMID 14517965. 
• "Congenital disorder of glycosylation Ic due to a de novo deletion and an hALG-6 mutation". Biochemical and Biophysical Research Communications 339 (3): 755–60. Jan 2006. doi:10.1016/j.bbrc.2005.11.073. PMID 16321363. 

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview
• Human ALG6 genome location and ALG6 gene details page in the UCSC Genome Browser.