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Literature summary for 2.4.1.11 extracted from

  • Diaz, A.; Diaz-Lobo, M.; Grados, E.; Guinovart, J.J.; Fita, I.; Ferrer, J.C.
    Lyase activity of glycogen synthase: is an elimination/addition mechanism a possible reaction pathway for retaining glycosyltransferases? (2012), IUBMB Life, 64, 649-658.
    View publication on PubMed
Search for more literature for 2.4.1.11

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21(DE3)/pG-Tf2 Pyrococcus abyssi

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme in complex with UDP-Glc, sitting drop vapor diffusion method, 0.002 ml of 5 mg/ml protein in 50-mM Tris-HCl, pH 7.4, with 10 mM UDP-Glc is mixed with 0.002 ml reservoir solution containing 0.1-M sodium citrate, pH 4.0, and 20-28% 2-methyl-2,4-pentanediol, 2 months, 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement Pyrococcus abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Pyrococcus abyssi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucose + [(1->4)-alpha-D-glucosyl]n Pyrococcus abyssi
-
 UDP + [(1->4)-alpha-D-glucosyl]n+1
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1 glycogen synthase performs a stepwise SNi-like mechanism, involving the concerted departure of the leaving group and the attack of the incoming nucleophile, via ion-pair intermediate 1,5-anhydro-D-arabino-hex-1-enitol or its tautomeric form, 1,5-anhydro-D-fructose, bound at the catalytic site. Even in the absence of a glucosyl acceptor, glycogen synthase promotes the formation of the cationic intermediate, which, by eliminating the proton of the adjacent C2 carbon atom, yields 1,5-anhydro-D-arabino-hex-1-enitol, overview Pyrococcus abyssi
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + [(1->4)-alpha-D-glucosyl]n
-
 Pyrococcus abyssi UDP + [(1->4)-alpha-D-glucosyl]n+1
-
 ?
UDP-glucose + [(1->4)-alpha-D-glucosyl]n glycogen synthase reacts with its glucosyl donor substrate, uridine 5'-diphosphoglucose to produce the scission of the covalent bond between the terminal phosphate oxygen of UDP and the sugar ring. UDP presence in the active site of the enzyme of a glucose-like derivative that lacks the exocyclic oxygen attached to the anomeric carbon Pyrococcus abyssi UDP + [(1->4)-alpha-D-glucosyl]n+1
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Pyrococcus abyssi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Pyrococcus abyssi