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Literature summary for 2.4.1.186 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
Search for more literature for 2.4.1.186

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Homo sapiens 5737
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P46976
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glycogenin
-
 Homo sapiens
glycogenin-1
-
 Homo sapiens
GYG1
-
 Homo sapiens

General Information

General Information Comment Organism
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