MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Arabidopsis thaliana col: glucan, water dikinaseInferred from experiment: GWD

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. 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

Taxonomic Range: Viridiplantae

Standard Gibbs Free Energy (ΔrG in kcal/mol): -11.887695Inferred by computational analysis [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.

Citations: [Ritte06, Ritte02]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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