ArticleThe Journal of biological chemistry2016
Structural Studies of Medicago truncatula Histidinol Phosphate Phosphatase from Inositol Monophosphatase Superfamily Reveal Details of Penultimate Step of Histidine Biosynthesis in Plants.
Article in The Journal of biological chemistry, 2016. 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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14 citing papers in PubMed, 23 citations in OpenAlex.
- Improving enzyme functional annotation by integrating in vitro and in silico approaches: The example of histidinol phosphate phosphatases.Protein science : a publication of the Protein Society · 2024Article
- Targeting imidazole-glycerol phosphate dehydratase in plants: novel approach for structural and functional studies, and inhibitor blueprinting.Frontiers in plant science · 2024Article
- Experimental and computational analysis of the ancestry of an evolutionary young enzyme from histidine biosynthesis.Protein science : a publication of the Protein Society · 2023Article
- Mobile forms of carbon in trees: metabolism and transport.Tree physiology · 2022Review
- Recognizing lysine-cysteine crosslinks in proteins.Protein science : a publication of the Protein Society · 2021Article
- Structural and mechanistic insights into the bifunctional HISN2 enzyme catalyzing the second and third steps of histidine biosynthesis in plants.Scientific reports · 2021Article
- The Function of Inositol Phosphatases in Plant Tolerance to Abiotic Stress.International journal of molecular sciences · 2019Review
- Crystallographic identification of spontaneous oxidation intermediates and products of protein sulfhydryl groups.Protein science : a publication of the Protein Society · 2019Article
- Comment on Wang's paper on the covalent Cys-X-Lys bridges.Protein science : a publication of the Protein Society · 2019Article
- Identification and structural characterization of a histidinol phosphate phosphatase fromThe Journal of biological chemistry · 2018Article
- Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NADScientific reports · 2017Article
- Reconstruction of amino acid biosynthetic pathways increases the productivity of 2-keto-L-gulonic acid in Ketogulonicigenium vulgare-Bacillus endophyticus consortium via genes screening.Journal of industrial microbiology & biotechnology · 2017Article
- Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures.Scientific reports · 2016Article
- On methylene-bridged cysteine and lysine residues in proteins.Protein science : a publication of the Protein Society · 2016Article
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2 authors at 2 institutions in 1 country.
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Abstract
The penultimate enzyme in the histidine biosynthetic pathway catalyzes dephosphorylation of l-histidinol 1-phosphate (HOLP) into l-histidinol. The recently discovered in Arabidopsis thaliana plant-type histidinol phosphate phosphatase (HPP) shares no homology with the two other HPP superfamilies known previously in prokaryotes and resembles myo-inositol monophosphatases (IMPases). In this work, identification of an HPP enzyme from a model legume, Medicago truncatula (MtHPP) was based on the highest sequence identity to A. thaliana enzyme. Biochemical assays confirmed that MtHPP was able to cleave inorganic phosphate from HOLP but not from d-myo-inositol-1-phosphate, the main substrate of IMPases. Dimers of MtHPP, determined by size exclusion chromatography, in the presence of CO2 or formaldehyde form mutual, methylene-bridged cross-links between Lys(158) and Cys(245) residues. Four high resolution crystal structures, namely complexes with HOLP (substrate), l-histidinol (product), and PO4 (3-) (by-product) as well as the structure showing the cross-linking between two MtHPP molecules, provide detailed structural information on the enzyme. Based on the crystal structures, the enzymatic reaction mechanism of IMPases is accustomed to fit the data for MtHPP. The enzymatic reaction, which requires Mg(2+) cations, is catalyzed mainly by amino acid residues from the N-terminal domain. The C-terminal domain, sharing little identity with IMPases, is responsible for the substrate specificity (i.e. allows the enzyme to distinguish between HOLP and d-myo-inositol-1-phosphate). Structural features, mainly the presence of a conserved Asp(246), allow MtHPP to bind HOLP specifically.
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