ArticleBiochemistry2013
Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Identification and characterization of alternative homologs of histidinol-phosphate phosphatase in Pseudomonas aeruginosa.BMC microbiology · 2025Article
- PHP-Family Diesterase fromBiochemistry · 2024Article
- 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
- Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria.International journal of molecular sciences · 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
- Biosynthesis of fosfomycin in pseudomonads reveals an unexpected enzymatic activity in the metallohydrolase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for recognition of distinct deaminated DNA lesions by endonuclease Q.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification and structural characterization of a histidinol phosphate phosphatase fromThe Journal of biological chemistry · 2018Article
- High-fidelity DNA replication in Mycobacterium tuberculosis relies on a trinuclear zinc center.Nature communications · 2017Article
- Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond.BMC microbiology · 2017Article
- An atypical phosphodiesterase capable of degrading haloalkyl phosphate diesters from Sphingobium sp. strain TCM1.Scientific reports · 2017Article
- Structural Studies of Medicago truncatula Histidinol Phosphate Phosphatase from Inositol Monophosphatase Superfamily Reveal Details of Penultimate Step of Histidine Biosynthesis in Plants.The Journal of biological chemistry · 2016Article
- Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks.Biochimica et biophysica acta · 2015Review
- Article
- Prospecting for unannotated enzymes: discovery of a 3',5'-nucleotide bisphosphate phosphatase within the amidohydrolase superfamily.Biochemistry · 2014Article
- Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus.Journal of the American Chemical Society · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
L-Histidinol phosphate phosphatase (HPP) catalyzes the hydrolysis of L-histidinol phosphate to L-histidinol and inorganic phosphate, the penultimate step in the biosynthesis of L-histidine. HPP from the polymerase and histidinol phosphatase (PHP) family of proteins possesses a trinuclear active site and a distorted (β/α)(7)-barrel protein fold. This group of enzymes is closely related to the amidohydrolase superfamily of enzymes. The mechanism of phosphomonoester bond hydrolysis by the PHP family of HPP enzymes was addressed. Recombinant HPP from Lactococcus lactis subsp. lactis that was expressed in Escherichia coli contained a mixture of iron and zinc in the active site and had a catalytic efficiency of ~10(3) M(-1) s(-1). Expression of the protein under iron-free conditions resulted in the production of an enzyme with a 2 order of magnitude improvement in catalytic efficiency and a mixture of zinc and manganese in the active site. Solvent isotope and viscosity effects demonstrated that proton transfer steps and product dissociation steps are not rate-limiting. X-ray structures of HPP were determined with sulfate, L-histidinol phosphate, and a complex of L-histidinol and arsenate bound in the active site. These crystal structures and the catalytic properties of variants were used to identify the structural elements required for catalysis and substrate recognition by the HPP family of enzymes within the amidohydrolase superfamily.
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