EC number:3.1.1.11

Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.1 Carboxylic-ester hydrolases
ID:3.1.1.11
Description:Pectinesterase.
Alternative Name: Pectin methylesterase.
Pectin methoxylase.
Pectin demethoxylase.
Prosite: PDOC00413;
PDB:
PDBScop
1QJV 8030602; 8042981; 8030602; 8042981;
1GQ8 8026430; 8038809;
3GRH
2NTQ
2NTP
 » show all
Cath: 2.160.20.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.1.11
BRENDA Enzyme Link: BRENDA 3.1.1.11
KEGG Enzyme Link: KEGG3.1.1.11
BioCyc Enzyme Link: BioCyc 3.1.1.11
ExPASy Enzyme Link: ExPASy3.1.1.11
EC2PDB Enzyme Link: EC2PDB 3.1.1.11
ExplorEnz Enzyme Link: ExplorEnz 3.1.1.11
PRIAM enzyme-specific profiles Link: PRIAM 3.1.1.11
IntEnz Enzyme Link: IntEnz 3.1.1.11
MEDLINE Enzyme Link: MEDLINE 3.1.1.11

EC number:3.1.1.11

MSA:

3.1.1.11;
Phylogenetic Tree:

3.1.1.11;
Uniprot:
M-CSA:
RHEA:22380 [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH3;+0:3].[OH2;+0:4]>>[*:1]-[OH;+0:2].[CH3;+0:3]-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
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 MA, D'Avino R, Amoresano A, Tuppo L, Carpentieri A, Carratore V, Tamburrini M, Giovane A, Pucci P, Camardella L2008 Apr17932919
A biochemical study of Pseudomonas prunicola Wormald. 1. Pectin esterase.Mills GB194916748520
Pectic substances and pectic enzymes.DEUEL H, STUTZ E195813605988