ArticleJournal of experimental botany2018
Catalytic and structural properties of pheophytinase, the phytol esterase involved in chlorophyll breakdown.
Article in Journal of experimental botany, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 33 citations in OpenAlex.
- Oxalic acid in root exudates confers lead tolerance in Medicago sativa L. via rhizosphere chelation and cellular detoxification.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- Regulatory Role of Jasmonate Signaling in Dark-, Drought-, and Salt-Induced Leaf Senescence.International journal of molecular sciences · 2026Review
- Bioactive Compounds, Antioxidant, and Antimicrobial Activity of Seeds and Mucilage of Non-Traditional Cocoas.Antioxidants (Basel, Switzerland) · 2025Article
- A family of α/β hydrolases removes phytol from chlorophyll metabolites for tocopherol biosynthesis in Arabidopsis.The Plant cell · 2025Article
- A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds.The Journal of biological chemistry · 2023Article
- Crystal structure and reaction mechanism of a bacterial Mg-dechelatase homolog from the Chloroflexi Anaerolineae.Protein science : a publication of the Protein Society · 2022Article
- Expression of a ChlorophyllInternational journal of molecular sciences · 2022Article
- Functional Characterization of the Pheophytinase Gene,Frontiers in plant science · 2021Article
- Insights into the structure and function of the rate-limiting enzyme of chlorophyll degradation through analysis of a bacterial Mg-dechelatase homolog.Computational and structural biotechnology journal · 2021Article
- Screening of key genes responsible for Pennisetum setaceum 'Rubrum' leaf color using transcriptome sequencing.PloS one · 2020Article
- Chlorophyll Oxidative Metabolism During the Phototrophic and Heterotrophic Growth ofAntioxidants (Basel, Switzerland) · 2019Article
- Characterization of the pheophorbide a oxygenase/phyllobilin pathway of chlorophyll breakdown in grasses.Planta · 2018Article
- Plant senescence: how plants know when and how to die.Journal of experimental botany · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During leaf senescence and fruit ripening, chlorophyll is degraded in a multistep pathway into linear tetrapyrroles called phyllobilins. A key feature of chlorophyll breakdown is the removal of the hydrophobic phytol chain that renders phyllobilins water soluble, an important prerequisite for their ultimate storage in the vacuole of senescent cells. Chlorophyllases had been considered for more than a century to catalyze dephytylation in vivo; however, this was recently refuted. Instead, pheophytinase was discovered as a genuine in vivo phytol hydrolase. While chlorophyllase acts rather unspecifically towards different porphyrin substrates, pheophytinase was shown to specifically dephytylate pheophytin, namely Mg-free chlorophyll. The aim of this work was to elucidate in detail the biochemical and structural properties of pheophytinase. By testing different porphyrin substrates with recombinant pheophytinase from Arabidopsis thaliana we show that pheophytinase has high specificity for the acid moiety of the ester bond, namely the porphyrin ring, while the nature of the alcohol, namely the phytol chain in pheophytin, is irrelevant. In silico modelling of the 3-dimensional structure of pheophytinase and subsequent analysis of site-directed pheophytinase mutant forms allowed the identification of the serine, histidine, and aspartic acid residues that compose the catalytic triad, a classical feature of serine-type hydrolases to which both pheophytinase and chlorophyllase belong. Based on substantial structural differences in the models of Arabidopsis pheophytinase and chlorophyllase 1, we discuss potential differences in the catalytic properties of these two phytol hydrolases.
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