ArticleFrontiers in plant science2018
Chloroplastic Serine Hydroxymethyltransferase From
Article in Frontiers in plant science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- The 'photosynthetic CCommunications biology · 2024Article
- Genome-wide identification of SHMT family genes in alfalfa (Medicago sativa) and its functional analyses under various abiotic stresses.BMC genomics · 2024Article
- CsSHMT3 gene enhances the growth and development in cucumber seedlings under salt stress.Plant molecular biology · 2024Article
- Structural insights into binding of polyglutamylated tetrahydrofolate by serine hydroxymethyltransferase 8 from soybean.Frontiers in plant science · 2024Article
- Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography.Communications chemistry · 2023Article
- Mapping of quantitative trait loci for the nutritional value of fresh market tomato.Functional & integrative genomics · 2023Article
- Characterization of thermostable serine hydroxymethyltransferase for β-hydroxy amino acids synthesis.Amino acids · 2023Article
- Genome-wide identification of3 Biotech · 2022Article
- The proteome of developing barley anthers during meiotic prophase I.Journal of experimental botany · 2022Article
- Metabolism and Regulatory Functions ofFrontiers in plant science · 2021Review
- Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode.The Journal of biological chemistry · 2020Article
- Structural basis of methotrexate and pemetrexed action on serine hydroxymethyltransferases revealed using plant models.Scientific reports · 2019Article
- Structural Study of Agmatine Iminohydrolase FromFrontiers in plant science · 2019Article
- Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) FromFrontiers in plant science · 2018Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Serine hydroxymethyltransferase (SHMT, EC 2.1.2.1) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme which catalyzes the reversible serine-to-glycine conversion in either a tetrahydrofolate-dependent or -independent manner. The enzyme is also responsible for the tetrahydrofolate-independent cleavage of other β-hydroxy amino acids. In addition to being an essential player in the serine homeostasis, SHMT action is the main source of activated one-carbon units, which links SHMT activity with the control of cell proliferation. In plants, studies of SHMT enzymes are more complicated than of those of, e.g., bacterial or mammalian origins because plant genomes encode multiple SHMT isozymes that are targeted to different subcellular compartments: cytosol, mitochondria, plastids, and nucleus. Here we report crystal structures of chloroplast-targeted SHMT from
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.