| EC |
4.2.2.27 |
| Accepted name: |
pectin monosaccharide-lyase |
| Reaction: |
(1,4-α-D-galacturonosyl methyl ester)n = (1,4-α-D-galacturonosyl methyl ester)n-1 + 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate |
| Other name(s): |
exo-pectin lyase; PLIII |
| Systematic name: |
poly(1,4-α-D-galacturonosyl methyl ester) non-reducing-end-monosaccharide-lyase |
| 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: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Pedrolli, D.B. and 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] |
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| [EC 4.2.2.27 created 2020] |
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