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. 2017 Jun 14;7:3533. doi: 10.1038/s41598-017-03807-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Enzymatic functions, domain architectures, and effectors of 3-phosphoglycerate dehydrogenase. (a) Schematic of the phosphorylated pathway; names of enzymes are underlined; PGDH, 3-phosphoglycerate dehydrogenase; PSAT, phosphoserine aminotransferase; PSP, phosphoserine phosphatase; 3-PHP, 3-phosphohydroxypyruvate; 3-PS, 3-phosphoserine; l-Glu, l-glutamate; 2-OG, 2-oxoglutarate; Pi, inorganic phosphate. (b) Domain architectures and effectors of PGDH; the domains of PGDH proteins from archaea [S. tokodaii (StPGDH)], bacteria [E. coli (EcPGDH) and M. tuberculosis (MtPGDH)], cyanobacterium [A. halophytica (AhPGDH)], mammals [R. norvegicus (RnPGDH) and Homo sapiens (HsPGDH)], and plant [A. thaliana (AtPGDHs)] are schematically shown with highlighted catalytic, ACT, and ASB domains. Because ACT domains of HsPGDH and RnPGDH are not functional, they are indicated in white. Numbers in parenthesis indicate references. In ref. 14, HsPGDH was not inhibited by serine, although the data were not shown (“No ? ” in the figure).