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Literature summary extracted from

  • Camiruaga, A.; Usabiaga, I.; Insausti, A.; Cocinero, E.; Leon, I.; Fernandez, J.
    Understanding the role of tyrosine in glycogenin (2017), Mol. Biosyst., 13, 1709-1712 .
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.186 cytoplasm
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 Homo sapiens 5737
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.186 UDP-alpha-D-glucose + glycogenin Homo sapiens
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 UDP + alpha-D-glucosylglycogenin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.186 Homo sapiens P46976
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.186 skeletal muscle
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 Homo sapiens
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.186 UDP-alpha-D-glucose + glycogenin
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 Homo sapiens UDP + alpha-D-glucosylglycogenin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.186 glycogenin
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 Homo sapiens
2.4.1.186 glycogenin-1
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 Homo sapiens
2.4.1.186 GYG1
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 Homo sapiens

General Information

EC Number General Information Comment Organism
2.4.1.186 additional information muscle glycogenin contains a single tyrosine, Tyr194, in covalent linkage with the first sugar unit, glucose, beta-phenyl-D-glucopyranoside (beta-PhGlc), confirming that tyrosine is fundamental for glycogen formation. Analysis of the mechanism for the early stages of the biosynthesis of glycogen. This macromolecule structure (PDB ID 3U2U) is constructed via the covalent attachment of glucose units to glycogenin, which remains covalently bonded to Tyr194 in a mature glycogen molecule. Isolation of the Tyr194 side chain in covalent linkage with glucose, of beta-phenyl-D-glucopyranoside, and examined the influence that the substitution of the tyrosine with different interacting reactants has on the preferred interaction sites, preferred interaction site for both alpha- and beta-Glc at body temperature is the 4-OH group of beta-PhGl, overview. The phenolic substituent of tyrosine is ideal, as it provides a rigid structure, acting as a hook for glucose, and the aromatic ring provides a tantalizing interacting environment that most molecules find entropically more favourable. The ability of glycogenin to elongate its glucan chain may reflect structural constraints both in the amino acid and at the catalytic site Homo sapiens