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Literature summary for 2.4.1.25 extracted from

  • Lu, Y.; Steichen, J.M.; Yao, J.; Sharkey, T.D.
    The role of cytosolic alpha-glucan phosphorylase in maltose metabolism and the comparison of amylomaltase in Arabidopsis and Escherichia coli (2006), Plant Physiol., 142, 878-889.
    View publication on PubMed
Search for more literature for 2.4.1.25

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Arabidopsis thaliana
expression in Escherichia coli Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1,4-alpha-D-glucan + 1,4-alpha-D-glucan Escherichia coli it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycan exists in Escherichia coli maltooligosaccharides
-
 ?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan Arabidopsis thaliana it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana maltooligosaccharides
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8RXD9
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-alpha-D-glucan + 1,4-alpha-D-glucan it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycan exists in Escherichia coli Escherichia coli maltooligosaccharides
-
 ?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana Arabidopsis thaliana maltooligosaccharides
-
 ?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan maltose and a highly branched, soluble heteroglycan are excellent substrates for DPE2 Escherichia coli maltooligosaccharide
-
 ?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
-
 Arabidopsis thaliana maltooligosaccharide
-
 ?

Synonyms

Synonyms Comment Organism
At2g40840
-
 Arabidopsis thaliana
disproportionating enzyme
-
 Escherichia coli
disproportionating enzyme
-
 Arabidopsis thaliana
DPE2
-
 Escherichia coli