Glycerol kinase
From Proteopedia
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| - | {{ | + | {{STRUCTURE_1r59| PDB=1r59 | SIZE=400| SCENE= |right| CAPTION=Glycerol kinase complex with reaction products ADP and glycerol 3-phosphate, [[1r59]] }} |
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Revision as of 08:09, 4 November 2012
Template:STRUCTURE 1r59
Glycerol kinase (GK) phosphorylates glycerol forming glycerol 3-phosphate (G3P) using Mg-ATP as phosphate source. GK is a key enzyme in glycerol uptake and metabolism. Mutations of GK gene cause GK deficiency syndrome. PK is a multi-subunit allosteric enzyme. Its activity can be inhibited by fructose 1,6-bisphosphate (FBP) and by the glucose-specific phosphocarrier IIA(Glc). PK cofactor is a Zn atom which binds to the dimer.
3D structures of glycerol kinase
1r59 – EncGK – Enterococcus casseliflavus
2dpn - GK - Thermus thermophilus
2d4w - GK - Cellulomonas
2zf5 - GK - Thermococcus kodakarensis
3gg4 – GK – Yersinia pseudotuberculosis
Glycerol kinase binary complex with glycerol
1xup - EncGK + glycerol
3flc, 3d7e, 3h3n, 3h46 - EncGK (mutant) + glycerol
3g25 - SaGK + glycerol– Staphylococcus aureus
4e1j – GK + glycerol – Sinorhizobium meliloti
1bu6, 3ezw - EcGK (mutant) + glycerol
Glycerol kinase ternary complex
1gla – EcGK + IIA(Glc) + glycerol – Escherichia coli
1glb - EcGK + IIA(Glc) + ADP + glycerol
1glc, 1gld, 1gle – EcGK + G3P + ADP
1glf - EcGK + phosphate + ADP + glycerol
1bo5 - EcGK + FBP + glycerol
1bot - EcGK + piperazine derivative + glycerol
1bwf, 1glj, 1gll - EcGK (mutant) + ATP analog + glycerol
3ge1 - SaGK + ADP + glycerol
3h3o - EncGK (mutant) + phosphate + glycerol
3h45 - EncGK (mutant) + phosphate + ethylene glycol
