EC 4.2.2.27 - Pectin monosaccharide-lyase

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IntEnz Enzyme Nomenclature
EC 4.2.2.27

Names

Accepted name:
pectin monosaccharide-lyase
Other name:
exo-pectin lyase
Systematic name:
poly(1,4-α-D-galacturonosyl methyl ester) non-reducing-end-monosaccharide-lyase

Reaction

Comments:

The enzyme, isolated from the fungus Aspergillus giganteus, acts on the non-reducing end of methyl-esterified polygalacturonan, releasing either 4-deoxy--L-threo-hex-4-enopyranuronate or 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate. The enzyme is stimulated by divalent cations, with Co2+ having the strongest effect. It is able to act on substrates as short as a disaccharide, and was active on substrates with degrees of methyl esterification ranging between 34% and 90%.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Pedrolli, D. B., Carmona, E. C.
    Purification and Characterization of a Unique Pectin Lyase from Aspergillus giganteus Able to Release Unsaturated Monogalacturonate during Pectin Degradation.
    Enzyme Res 2014 : 353915 (2014). [PMID: 25610636]

[EC 4.2.2.27 created 2020]