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Glycerol kinase

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==3D structures of glycerol kinase==
==3D structures of glycerol kinase==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[1r59]] – EncGK – ''Enterococcus casseliflavus''<br />
[[1r59]] – EncGK – ''Enterococcus casseliflavus''<br />

Revision as of 08:43, 10 March 2013

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

Updated on 10-March-2013

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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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