GLUT1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The GLUT1 transporter has one known <scene name='91/910668/Glut1_n-glycosylation/1'>N-linked glycosylation</scene> site at Asn 45. This glycosylation site is thought to be important for glucose binding to the extracellular portion of the transporter. Mutations in the GLUT1 transporter from Asn 45 to an Asp, Tyr, or Gln residue have been shown to increase the Km of the enzyme.<ref>PMID:1761560</ref> | + | The GLUT1 transporter has one known <scene name='91/910668/Glut1_n-glycosylation/1'>N-linked glycosylation</scene> site at Asn 45 and varied molecular weights of the GLUT1 transporter suggest different isoforms of the enzyme are expressed in different cells. This glycosylation site is thought to be important for glucose binding to the extracellular portion of the transporter. Mutations in the GLUT1 transporter from Asn 45 to an Asp, Tyr, or Gln residue have been shown to increase the Km of the enzyme.<ref>PMID:1761560</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 20:17, 25 April 2022
Structure
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References
Pragallapati S, Manyam R. Glucose transporter 1 in health and disease. J Oral Maxillofac Pathol. 2019 Sep-Dec;23(3):443-449. doi: 10.4103/jomfp.JOMFP_22_18. PMID: 31942129; PMCID: PMC6948067.
Koepsell H. Glucose transporters in brain in health and disease. Pflugers Arch. 2020 Sep;472(9):1299-1343. doi: 10.1007/s00424-020-02441-x. Epub 2020 Aug 13. PMID: 32789766; PMCID: PMC7462931.
Asano T, Katagiri H, Takata K, Lin JL, Ishihara H, Inukai K, Tsukuda K, Kikuchi M, Hirano H, Yazaki Y, et al. The role of N-glycosylation of GLUT1 for glucose transport activity. J Biol Chem. 1991 Dec 25;266(36):24632-6. PMID: 1761560.
