Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.2 Acting on polysaccharides
ID:4.2.2.6
Description:Oligogalacturonide lyase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.2.6
BRENDA Enzyme Link: BRENDA 4.2.2.6
KEGG Enzyme Link: KEGG4.2.2.6
BioCyc Enzyme Link: BioCyc 4.2.2.6
ExPASy Enzyme Link: ExPASy4.2.2.6
EC2PDB Enzyme Link: EC2PDB 4.2.2.6
ExplorEnz Enzyme Link: ExplorEnz 4.2.2.6
PRIAM enzyme-specific profiles Link: PRIAM 4.2.2.6
IntEnz Enzyme Link: IntEnz 4.2.2.6
MEDLINE Enzyme Link: MEDLINE 4.2.2.6
MSA:

4.2.2.6;

Phylogenetic Tree:

4.2.2.6;

Uniprot:
M-CSA:
RHEA:20269 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
RULE(radius=1) [*:1]-[CH;+0:2]1-[O;H0;+0:3]-[CH;+0:4](-[OH;+0:5])-[*:6]-[*:7]-[CH;+0:8]-1-[O;H0;+0:9]-[CH;+0:10]1-[*:11]-[*:12]-[CH;+0:13]=[C;H0;+0:14](-[*:15])-[O;H0;+0:16]-1>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[CH2;+0:8]-[*:7]-[*:6]-[CH;+0:4]=[O;H0;+0:5].[*:15]-[C;H0;+0:14](=[O;H0;+0:16])-[CH2;+0:13]-[*:12]-[*:11]-[CH;+0:10]=[O;H0;+0:9]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The active site of oligogalacturonate lyase provides unique insights into cytoplasmic oligogalacturonate beta-elimination.Abbott DW, Gilbert HJ, Boraston AB2010 Dec 1020851883
Performance of selected microbial pectinases on synthetic monomethyl-esterified di- and trigalacturonates.Kester HC, Magaud D, Roy C, Anker D, Doutheau A, Shevchik V, Hugouvieux-Cotte-Pattat N, Benen JA, Visser J1999 Dec 2410601263