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Glycerol kinase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' caption='Glycerol kinase complex with glycerol (PDB entry [[1xup]])' scene='48/487479/Cv/1'> |
== Function == | == Function == | ||
'''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<ref>PMID:10759857</ref>. | '''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<ref>PMID:10759857</ref>. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | GK active site is located in a cleft between two domains<ref>PMID:14717590</ref>. | + | <scene name='48/487479/Cv/3'>GK active site</scene> is located in a cleft between two domains<ref>PMID:14717590</ref>. |
</StructureSection> | </StructureSection> | ||
==3D structures of glycerol kinase== | ==3D structures of glycerol kinase== | ||
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**[[2dpn]] - GK - ''Thermus thermophilus''<br /> | **[[2dpn]] - GK - ''Thermus thermophilus''<br /> | ||
**[[2d4w]] - GK - ''Cellulomonas''<br /> | **[[2d4w]] - GK - ''Cellulomonas''<br /> | ||
| - | **[[2zf5]] - | + | **[[2zf5]] - TkGK - ''Thermococcus kodakarensis''<br /> |
**[[3gg4]] – GK – ''Yersinia pseudotuberculosis''<br /> | **[[3gg4]] – GK – ''Yersinia pseudotuberculosis''<br /> | ||
**[[3wxi]] – TbGK – ''Trypanosoma brucei gambiense''<br /> | **[[3wxi]] – TbGK – ''Trypanosoma brucei gambiense''<br /> | ||
| + | **[[6zq5]], [[6zq8]] – CtGK – ''Chaetonium thermophilum'' <br /> | ||
| - | *Glycerol kinase binary complex | + | *Glycerol kinase binary complex |
**[[1xup]] - EncGK + glycerol<br /> | **[[1xup]] - EncGK + glycerol<br /> | ||
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**[[4e1j]] – GK + glycerol – ''Sinorhizobium meliloti''<br /> | **[[4e1j]] – GK + glycerol – ''Sinorhizobium meliloti''<br /> | ||
**[[1bu6]], [[3ezw]] - EcGK (mutant) + glycerol<br /> | **[[1bu6]], [[3ezw]] - EcGK (mutant) + glycerol<br /> | ||
| - | **[[3wxk]] – TbGK + glycerol <br /> | + | **[[3wxk]], [[6j9x]], [[6jae]], [[6jaf]] – TbGK + glycerol <br /> |
| + | **[[6zq4]], [[6zq6]], [[6zq7]] – CtGK + glycerol <br /> | ||
| + | **[[6k76]] – TkGK + AMPPNP<br /> | ||
| + | **[[6k78]], [[6k79]] – TkGK + glycerol <br /> | ||
*Glycerol kinase ternary complex | *Glycerol kinase ternary complex | ||
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**[[3h45]] - EncGK (mutant) + phosphate + ethylene glycol<br /> | **[[3h45]] - EncGK (mutant) + phosphate + ethylene glycol<br /> | ||
**[[3wxj]] – TbGK + glycerol + G3P<br /> | **[[3wxj]] – TbGK + glycerol + G3P<br /> | ||
| - | **[[3wxl]] – TbGK + glycerol + ADP<br /> | + | **[[3wxl]], [[6j9v]] – TbGK + glycerol + ADP<br /> |
| + | **[[6j9q]] – TbGK + glycerol + AMPPNP<br /> | ||
| + | **[[5azi]], [[5azj]] – TbGK + glycerol + nitrophenyl-phosphate<br /> | ||
| + | **[[5gn5]], [[5gn6]] – TbGK + glycerol + coumarin derivative<br /> | ||
| + | **[[6ude]] – GK + glycerol + ADP – ''Elizabethkingia anophelis''<br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D structures of glycerol kinase
Updated on 11-August-2021
References
- ↑ Kralova I, Rigden DJ, Opperdoes FR, Michels PA. Glycerol kinase of Trypanosoma brucei. Cloning, molecular characterization and mutagenesis. Eur J Biochem. 2000 Apr;267(8):2323-33. PMID:10759857
- ↑ Sehgal A, Stack J. Complex glycerol kinase deficiency: an X-linked disorder associated with adrenal hypoplasia congenita. Indian J Pediatr. 2005 Jan;72(1):67-9. PMID:15684452
- ↑ Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J. Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation. Biochemistry. 2004 Jan 20;43(2):362-73. PMID:14717590 doi:10.1021/bi034258o
