Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.1 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 PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information enzyme knockout mutant, no visible phenotype of plants, but nighttime maltose level increases four times Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Arabidopsis thaliana 5829
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9SD76
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + alpha-D-glucose 1-phosphate
-
Arabidopsis thaliana amylopectin + phosphate
-
?
dextrin + alpha-D-glucose 1-phosphate
-
Arabidopsis thaliana dextrin + phosphate
-
?
glycogen + alpha-D-glucose 1-phosphate
-
Arabidopsis thaliana glycogen + phosphate
-
?

Synonyms

Synonyms Comment Organism
alpha-glucan phosphorylase H
-
Arabidopsis thaliana
starch phosphorylase H
-
Arabidopsis thaliana