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Literature summary extracted from

  • Senechal, F.; Habrylo, O.; Hocq, L.; Domon, J.M.; Marcelo, P.; Lefebvre, V.; Pelloux, J.; Mercadante, D.
    Structural and dynamical characterization of the pH-dependence of the pectin methylesterase-pectin methylesterase inhibitor complex (2017), J. Biol. Chem., 292, 21538-21547 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.11 gene PME3, quantitative real-time RT-PCR enzyme expression analysis Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.11 additional information construction of Atpme3-1 loss-of-function mutants, phenotypes with earlier germination and reduction of root hair production compared to wild-type, overview. A PME isoform with a pI 9.6 is lacking in all organs of the Atpme3-1 mutant, and loss of AtPME3 activity in the mutant cotyledon triggers the expression of the other PME isoform migrating at gpI 9.2. Altered Genome regulation in the mutant, overview. Genes encoding proteins putatively involved in cell wall organization and remodeling are mainly downregulated in hypocotyls of the Atpme3-1 mutant. Atpme3-1 seedlings display no specific phenotype except an increased adventitious rooting Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.11 pectin methylesterase inhibitor 7 PMEI7, inhibits the enzyme only at pH 5.0, not at pH 6.3-7.5, re-incubating the sample at pH values where the inhibitory capacity of AtPMEI7 is not expected, fully restores AtPME3 activity. PME3 enzyme-bound complex structure analysis, stability of the AtPME3-AtPMEI7 complex at acidic and neutral pH, overview. The mechanism of competition between intramolecular and intermolecular contacts is not isolated to a single pair of residues. Changes in the protonation of amino acids at the complex interface shift the network of interacting residues between intermolecular and intramolecular. These shifts ultimately regulate the stability of the PME3-PMEI7 complex and the inhibition of the PME as a function of the pH. Analysis of the conformational dynamics of the PMEI helices reveals a consistent twist of helix alphaII, which is mostly involved in the binding of AtPME3. The dihedral space explored by helix alphaII reveals the presence of several populations at pH 7.0, with values of psi dihedral angles shifting toward regions of the Ramachandran plot that do not characterize alpha-helices. PMEI7 mutated version E68A (as the wild-type protein) is able to inhibit PME activity, whereas E75A is not Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.11 cell wall AtPME3 is a ubiquitous cell wall pectin methylesterase Arabidopsis thaliana 5618
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.11 pectin + n H2O Arabidopsis thaliana
-
 n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O Arabidopsis thaliana Col-0
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 n methanol + pectate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.11 Arabidopsis thaliana O49006
-
-
3.1.1.11 Arabidopsis thaliana Col-0 O49006
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.11 hypocotyl
-
 Arabidopsis thaliana
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3.1.1.11 root
-
 Arabidopsis thaliana
-
3.1.1.11 seed
-
 Arabidopsis thaliana
-
3.1.1.11 seedling
-
 Arabidopsis thaliana
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.11 pectin + n H2O
-
 Arabidopsis thaliana n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O substrate is Citrus pectin with 82% degree of methylesterification Arabidopsis thaliana n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O
-
 Arabidopsis thaliana Col-0 n methanol + pectate
-
 ?
3.1.1.11 pectin + n H2O substrate is Citrus pectin with 82% degree of methylesterification Arabidopsis thaliana Col-0 n methanol + pectate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.11 AtPME3
-
 Arabidopsis thaliana
3.1.1.11 pectin methylesterase
-
 Arabidopsis thaliana
3.1.1.11 PME3
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 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.11 25
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.11 7.5
-
 assay at Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
3.1.1.11 evolution in Arabidopsis thaliana, 66 PMEs and a similarly high number of pectin methylesterase inhibitors, PMEIs, have so far been identified Arabidopsis thaliana
3.1.1.11 malfunction Atpme3-1 loss-of-function mutants exhibit phenotypes distinct from the wild-type, and show earlier germination and reduction of root hair production, correlated with the accumulation of a 21.5-kDa protein in the different organs of 4-day-old Atpme3-1 seedlings grown in the dark, as well as in 6-week-old mutant plants. Microarray analysis shows significant downregulation of the genes encoding several pectin-degrading enzymes and enzymes involved in lipid and protein metabolism in the hypocotyl of 4-day-old dark grown mutant seedlings. Accordingly, there is a decrease in proteolytic activity of the mutant as compared with the wild-type. Among the genes specifying seed storage proteins, two encoding cruciferins are upregulated. Overexpression of four cruciferin genes in the mutant Atpme3-1, in which precursors of the alpha- and beta-subunits of CRUCIFERIN accumulate Arabidopsis thaliana
3.1.1.11 physiological function regulation of enzyme PME may control the physical properties and structure of the plant cell wall. Evidence for a link between AtPME3, present in the cell wall, and CRUCIFERIN metabolism that occurs in vacuoles is provided Arabidopsis thaliana