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Glycerate kinase

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{{STRUCTURE_1to6| PDB=1to6 | SIZE=400| SCENE=Glycerate_kinase/Glycerate_kinase/1|right|CAPTION=Glycerate kinase dimer complex with SO4 ions, [[1to6]] }}
{{STRUCTURE_1to6| PDB=1to6 | SIZE=400| SCENE=Glycerate_kinase/Glycerate_kinase/1|right|CAPTION=Glycerate kinase dimer complex with SO4 ions, [[1to6]] }}
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'''Glycerate kinase''' (GK) catalyzes the conversion of ATP + glycerate to ADP + 3-phospho-glycerate. GK participates in the metabolic pathways of serine/glycine/threonine, glycolipid and glyoxylate-dicarboxylate. GK is the last step in the pathway which starts with glucose and ends with 2-phosphoglycerate.
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'''Glycerate kinase''' (GK) catalyzes the conversion of ATP + glycerate to ADP + 3-phospho-glycerate. GK participates in the metabolic pathways of serine/glycine/threonine, glycolipid and glyoxylate-dicarboxylate. GK is the last step in the pathway which starts with glucose and ends with 2-phosphoglycerate<ref>PMID:5325263</ref>.
== 3D Structures of glycerate kinase ==
== 3D Structures of glycerate kinase ==
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[[1to6]] – GK – ''Neisseria meningitides''
[[1to6]] – GK – ''Neisseria meningitides''
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 07:26, 13 March 2016

Template:STRUCTURE 1to6

Glycerate kinase (GK) catalyzes the conversion of ATP + glycerate to ADP + 3-phospho-glycerate. GK participates in the metabolic pathways of serine/glycine/threonine, glycolipid and glyoxylate-dicarboxylate. GK is the last step in the pathway which starts with glucose and ends with 2-phosphoglycerate[1].

3D Structures of glycerate kinase

Updated on 13-March-2016

1to6 – GK – Neisseria meningitides

References

  1. Doughty CC, Hayashi JA, Guenther HL. Purification and properties of D-glycerate 3-kinase from Escherichia coli. J Biol Chem. 1966 Feb 10;241(3):568-72. PMID:5325263

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Eran Hodis

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