Enzymes
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Name help_outline
[(1→4)-α-D-galacturonosyl methyl ester](n)
Identifier
CHEBI:140522
Charge
0
Formula
(C7H10O6)n.H2O
Search links
Involved in 2 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:14573Polymer name: [(1→4)-α-D-galacturonosyl methyl ester](n)Polymerization index help_outline nFormula H2O(C7H10O6)nCharge (0)(0)nMol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
[(1→4)-α-D-galacturonosyl](n)
Identifier
CHEBI:140523
Charge
-1
Formula
(C6H7O6)n.H2O
Search links
Involved in 5 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:14570Polymer name: [(1→4)-α-D-galacturonosyl](n)Polymerization index help_outline nFormula H2O(C6H7O6)nCharge (0)(-1)nMol File for the polymer
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- Name help_outline methanol Identifier CHEBI:17790 (CAS: 67-56-1) help_outline Charge 0 Formula CH4O InChIKeyhelp_outline OKKJLVBELUTLKV-UHFFFAOYSA-N SMILEShelp_outline CO 2D coordinates Mol file for the small molecule Search links Involved in 46 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:22380 | RHEA:22381 | RHEA:22382 | RHEA:22383 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor.
Ciardiello M.A., D'Avino R., Amoresano A., Tuppo L., Carpentieri A., Carratore V., Tamburrini M., Giovane A., Pucci P., Camardella L.
Pectin methylesterase (PME) from kiwi fruit (Actinidia deliciosa) is a glycoprotein, showing an apparent molecular mass of 50 kDa upon size exclusion chromatography and SDS-PAGE. The primary structure, elucidated by direct sequencing of the protein, comprises 321 amino acid residues providing a mo ... >> More
Pectin methylesterase (PME) from kiwi fruit (Actinidia deliciosa) is a glycoprotein, showing an apparent molecular mass of 50 kDa upon size exclusion chromatography and SDS-PAGE. The primary structure, elucidated by direct sequencing of the protein, comprises 321 amino acid residues providing a molecular mass of 35 kDa. The protein has an acetylated Thr residue at the amino terminus and five N-glycosylation consensus sequences, four of which are actually glycosylated. A careful investigation of the oligosaccharide structures demonstrated that PME glycans belong to complex type oligosaccharides essentially consisting of xylosylated polyfucosylated biantennary structures. Alignment with known mature plant PME sequences indicates that the postulated active site residues are conserved. Kiwi PME activity is inhibited following the interaction with the proteinaceous inhibitor PMEI, isolated from the same source. Gel-filtration experiments show that kiwi PME/PMEI complex is stable in a large pH range and dissociates only at pH 10.0. Modeling of the interaction with the inhibitor was performed by using the crystal structure of the complex between kiwi PMEI and tomato PME as a template. The model shows that the binding site is the same reported for tomato PME. However, additional salt link interactions are found to connect the external loops of kiwi PME to PMEI. This finding may explain the higher pH stability of the complex formed by the two kiwi proteins respect to that formed by PMEI and tomato PME. << Less
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A biochemical study of Pseudomonas prunicola Wormald. 1. Pectin esterase.
Mills G.B.
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Pectic substances and pectic enzymes.
DEUEL H., STUTZ E.
Adv Enzymol Relat Subj Biochem 20:341-382(1958) [PubMed] [EuropePMC]