KEGG   ENZYME: 4.2.2.27
Entry
EC 4.2.2.27                 Enzyme                                 

Name
pectin monosaccharide-lyase;
exo-pectin lyase;
PLIII
Class
Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
Sysname
poly(1,4-alpha-D-galacturonosyl methyl ester) non-reducing-end-monosaccharide-lyase
Reaction(IUBMB)
(1,4-alpha-D-galacturonosyl methyl ester)n = (1,4-alpha-D-galacturonosyl methyl ester)n-1 + 4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate
Substrate
(1,4-alpha-D-galacturonosyl methyl ester)n
Product
(1,4-alpha-D-galacturonosyl methyl ester)n-1;
4-deoxy-6-O-methyl-L-threo-hex-4-enopyranuronate
Comment
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%.
History
EC 4.2.2.27 created 2020
Reference
1  [PMID:25610636]
  Authors
Pedrolli DB, Carmona EC
  Title
Purification and Characterization of a Unique Pectin Lyase from Aspergillus giganteus Able to Release Unsaturated Monogalacturonate during Pectin Degradation.
  Journal
Enzyme Res 2014:353915 (2014)
DOI:10.1155/2014/353915
Other DBs
ExplorEnz - The Enzyme Database: 4.2.2.27
IUBMB Enzyme Nomenclature: 4.2.2.27
ExPASy - ENZYME nomenclature database: 4.2.2.27
BRENDA, the Enzyme Database: 4.2.2.27

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