ArticleThe Journal of biological chemistry2016
Structure and Properties of a Non-processive, Salt-requiring, and Acidophilic Pectin Methylesterase from Aspergillus niger Provide Insights into the Key Determinants of Processivity Control.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 37 citations in OpenAlex.
- Crystal Structure of the Multidomain Pectin Methylesterase PmeC5 fromBiomolecules · 2025Article
- Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from RumenInternational journal of molecular sciences · 2023Article
- Uncovering the interactions between PME and PMEI at the gene and protein levels: Implications for the design of specific PMEI.Journal of molecular modeling · 2023Article
- Arabidopsis root responses to salinity depend on pectin modification and cell wall sensing.Development (Cambridge, England) · 2022Article
- Biochemical characterization and molecular insights into substrate recognition of pectin methylesterase fromComputational and structural biotechnology journal · 2022Article
- Characterization of anFrontiers in microbiology · 2021Article
- Development of an Innovative Process for High-Temperature Fruit Juice Extraction Using a Novel Thermophilic Endo-Polygalacturonase FromFrontiers in microbiology · 2020Article
- Structural determination of Enzyme-Graphene Nanocomposite Sensor Material.Scientific reports · 2019Article
- Resolving solution conformations of the model semi-flexible polyelectrolyte homogalacturonan using molecular dynamics simulations and small-angle x-ray scattering.The European physical journal. E, Soft matter · 2019Article
- Molecular Cloning, Expression and Characterization of Pectin Methylesterase (CtPME) from Clostridium thermocellum.Molecular biotechnology · 2017Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many pectin methylesterases (PMEs) are expressed in plants to modify plant cell-wall pectins for various physiological roles. These pectins are also attacked by PMEs from phytopathogens and phytophagous insects. The de-methylesterification by PMEs of the O6-methyl ester groups of the homogalacturonan component of pectin, exposing galacturonic acids, can occur processively or non-processively, respectively, describing sequential versus single de-methylesterification events occurring before enzyme-substrate dissociation. The high resolution x-ray structures of a PME from Aspergillus niger in deglycosylated and Asn-linked N-acetylglucosamine-stub forms reveal a 10⅔-turn parallel β-helix (similar to but with less extensive loops than bacterial, plant, and insect PMEs). Capillary electrophoresis shows that this PME is non-processive, halophilic, and acidophilic. Molecular dynamics simulations and electrostatic potential calculations reveal very different behavior and properties compared with processive PMEs. Specifically, uncorrelated rotations are observed about the glycosidic bonds of a partially de-methyl-esterified decasaccharide model substrate, in sharp contrast to the correlated rotations of processive PMEs, and the substrate-binding groove is negatively not positively charged.
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