Phosphoglycerate dehydrogenase: Difference between revisions
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<StructureSection load='3ddn' size='350' side='right' caption='Phosphoglycerate dehydrogenase dimer complex with hydroxypyruvic acid phosphate and tartar ate (PDB entry [[3ddn]])' scene=''> | |||
== Function == | == Function == | ||
'''Phosphoglycerate dehydrogenase''' (PGDH) catalyzes the conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate. This is the first step of serine biosynthesis. NAD is used as cofactor. In some cancer cells there is an elevation in PGDH level. | '''Phosphoglycerate dehydrogenase''' (PGDH) catalyzes the conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate. This is the first step of serine biosynthesis<ref>PMID:11567059</ref>. NAD is used as cofactor. | ||
== Relevance == | |||
In some cancer cells there is an elevation in PGDH level and hence an increase in serine biosynthesis<ref>PMID:26831078</ref>. | |||
== Structural highlights == | == Structural highlights == | ||
The active site of ''Mycobacterium tuberculosis'' located in the cleft between the substrate and the NAD-binding domains contains the catalytic dyad Glu:His and the substrate<ref>PMID:18627175</ref>. | |||
See [[Rossmann fold]]. | See [[Rossmann fold]]. | ||
</StructureSection> | |||
==3D structures of phosphoglycerate dehydrogenase== | ==3D structures of phosphoglycerate dehydrogenase== | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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**[[2pa3]] - EcPGDH (mutant) + serine + NAD | **[[2pa3]] - EcPGDH (mutant) + serine + NAD | ||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 13:11, 27 June 2016
FunctionPhosphoglycerate dehydrogenase (PGDH) catalyzes the conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate. This is the first step of serine biosynthesis[1]. NAD is used as cofactor. RelevanceIn some cancer cells there is an elevation in PGDH level and hence an increase in serine biosynthesis[2]. Structural highlightsThe active site of Mycobacterium tuberculosis located in the cleft between the substrate and the NAD-binding domains contains the catalytic dyad Glu:His and the substrate[3]. See Rossmann fold. |
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3D structures of phosphoglycerate dehydrogenase3D structures of phosphoglycerate dehydrogenase
ReferencesReferences
- ↑ Yamasaki M, Yamada K, Furuya S, Mitoma J, Hirabayashi Y, Watanabe M. 3-Phosphoglycerate dehydrogenase, a key enzyme for l-serine biosynthesis, is preferentially expressed in the radial glia/astrocyte lineage and olfactory ensheathing glia in the mouse brain. J Neurosci. 2001 Oct 1;21(19):7691-704. PMID:11567059
- ↑ Mullarky E, Lucki NC, Beheshti Zavareh R, Anglin JL, Gomes AP, Nicolay BN, Wong JC, Christen S, Takahashi H, Singh PK, Blenis J, Warren JD, Fendt SM, Asara JM, DeNicola GM, Lyssiotis CA, Lairson LL, Cantley LC. Identification of a small molecule inhibitor of 3-phosphoglycerate dehydrogenase to target serine biosynthesis in cancers. Proc Natl Acad Sci U S A. 2016 Feb 16;113(7):1778-83. doi:, 10.1073/pnas.1521548113. Epub 2016 Feb 1. PMID:26831078 doi:http://dx.doi.org/10.1073/pnas.1521548113
- ↑ Dey S, Burton RL, Grant GA, Sacchettini JC. Structural analysis of substrate and effector binding in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase. Biochemistry. 2008 Aug 12;47(32):8271-82. Epub 2008 Jul 16. PMID:18627175 doi:10.1021/bi800212b