Glycogenin

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Glycogenin
Mass / length primary structure 349 amino acids
Secondary to quaternary structure Homodimer
Cofactor manganese
Isoforms GN-1L, GN-1, GN-1S, GN-2α, GN-2β, GN-2γ, GN-2δ, GN-2ε, GN-2ζ
Identifier
Gene name (s) GYG1 , GYG2
External IDs
Enzyme classification
EC, category 2.4.1.186 glycosyl transferase
Response type Transfer of a glucose residue
Substrate Glucosyl n -Glycogenin + UDP-glucose (n = 0-12)
Products Glucosyl n + 1 -Glycogenin + UDP
Occurrence
Homology family Glycogenin
Parent taxon Mushrooms / multicellular cells

Glycogenins are enzymes that attach glucose residues to themselves - the polysaccharide chain can be up to 13 glucose units long. This reaction is necessary to get the production of long-chain polysaccharides , especially glycogen , going, because the enzyme glycogen synthase can only work if short chains are already present. Glycogenins are found in mushrooms and multicellular organisms . Humans have two homologous genes , each of which allows for multiple isoforms of the enzyme located in different tissue types. Glycogenin is tightly bound to glycogen synthase , so it can be called its cofactor . Mutations in the GYG1 gene are responsible for an inherited glycogen storage disease .

Catalyzed reactions

Glycogenin + +UDP glucose  
Glc-glycogeninUDP

Glycogenin catalyzes the addition of glucose to itself by binding the first UDP-glucose , formed from UTP and glucose-1-phosphate, to the Tyr-194 residue of its active site. This creates UDP .

Glc-glycogenin+ +UDP glucose
Glc (n) glycogeninUDP

The enzyme then lines up further glucose residues up to a certain limit (approx. 5-13), after which the glycogen synthase takes over the further polymerization. The glycogenin remains bound to the glycogen chain. After possible breakdown of the chain, the enzyme is available as a germ cell for renewed glycogen synthesis. H. it is not dismantled.

See also

Individual evidence

  1. UniProt P46976 , UniProt O15488
  2. Skurat AV, Dietrich AD, Roach PJ: Interaction between glycogenin and glycogen synthase . In: Arch. Biochem. Biophys. . 456, No. 1, December 2006, pp. 93-7. doi : 10.1016 / j.abb.2006.09.024 . PMID 17055998 . PMC 1769445 (free full text).
  3. Hurley TD, Walls C, Bennett JR, Roach PJ, Wang M: Direct detection of glycogenin reaction products during glycogen initiation . In: Biochem. Biophys. Res. Commun. . 348, No. 2, September 2006, pp. 374-8. doi : 10.1016 / j.bbrc.2006.07.106 . PMID 16889748 . PMC 1635985 (free full text).
  4. Wilson RJ, Gusba JE, Robinson DL, Graham TE: Glycogenin protein and mRNA expression in response to changing glycogen concentration in exercise and recovery . In: Am. J. Physiol. Endocrinol. Metab. . 292, No. 6, June 2007, pp. E1815-22. doi : 10.1152 / ajpendo.00598.2006 . PMID 17311895 .

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