|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: α-glucan, water dikinase
Enzyme Commission Synonyms: starch-related R1 protein, GWD
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -11.887695 [Latendresse13]
Enzyme Commission Summary:
ATP appears to be the only phosphate donor.
No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate.
The protein phosphorylates glucans at both the C-6 and C-3 position of the glucosyl residues.
The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan.
Ritte02: Ritte G, Lloyd JR, Eckermann N, Rottmann A, Kossmann J, Steup M (2002). "The starch-related R1 protein is an alpha -glucan, water dikinase." Proc Natl Acad Sci U S A 99(10);7166-71. PMID: 12011472
Ritte06: Ritte G, Heydenreich M, Mahlow S, Haebel S, Kotting O, Steup M (2006). "Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases." FEBS Lett 580(20);4872-6. PMID: 16914145
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