|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
Enzymes and Genes:
|Arabidopsis thaliana col:||glucan, water dikinase: GWD|
In Pathway: starch degradation II
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
Reaction Locations: chloroplast stroma
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Mass balance status: Marked as unbalanced.
Enzyme Commission Primary Name: α-glucan, water dikinase
Enzyme Commission Synonyms: starch-related R1 protein, GWD
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.
Fettke09: Fettke J, Hejazi M, Smirnova J, Hochel E, Stage M, Steup M (2009). "Eukaryotic starch degradation: integration of plastidial and cytosolic pathways." J Exp Bot 60(10);2907-22. PMID: 19325165
Hejazi08: Hejazi M, Fettke J, Haebel S, Edner C, Paris O, Frohberg C, Steup M, Ritte G (2008). "Glucan, water dikinase phosphorylates crystalline maltodextrins and thereby initiates solubilization." Plant J 55(2);323-34. PMID: 18419779
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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