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Glycerate kinase
From Proteopedia
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| + | <StructureSection load='1to6' size='350' side='right' caption='Glycerate kinase dimer complex with sulfate ions (PDB code [[1to6]]).' scene='Glycerate_kinase/Glycerate_kinase/1'> | ||
== Function == | == Function == | ||
'''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>. | '''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>. | ||
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== Disease == | == Disease == | ||
Mutation in GK is the cause of inherited D-glyceric acidemia) (D-glyceric aciduria)<ref>PMID:20949620</ref>. | Mutation in GK is the cause of inherited D-glyceric acidemia) (D-glyceric aciduria)<ref>PMID:20949620</ref>. | ||
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== 3D Structures of glycerate kinase == | == 3D Structures of glycerate kinase == | ||
Revision as of 21:05, 19 October 2017
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3D Structures of glycerate kinase
Updated on 19-October-2017
1to6 – GK – Neisseria meningitides
2b8n – GK – Thermotoga maritima
1x3l – GK – Pyrococcus horikoshii
3cwc – GK – Salmonella enterica
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
- ↑ Sass JO, Fischer K, Wang R, Christensen E, Scholl-Burgi S, Chang R, Kapelari K, Walter M. D-glyceric aciduria is caused by genetic deficiency of D-glycerate kinase (GLYCTK). Hum Mutat. 2010 Dec;31(12):1280-5. doi: 10.1002/humu.21375. Epub 2010 Nov 9. PMID:20949620 doi:http://dx.doi.org/10.1002/humu.21375
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