Glycerate kinase
From Proteopedia
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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]] }} | ||
| - | '''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. | + | '''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'' | ||
| - | + | == References == | |
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:26, 13 March 2016
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
- ↑ 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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