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Literature summary extracted from

  • Myers, D.; Matheson, N.K.
    Affinity purification and kinetics of pea cotyledon starch phosphorylases (1991), Phytochemistry, 30, 1079-1087.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 glucose 1-phosphate not inhibited Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.1 additional information
-
additional information kinetic data Pisum sativum
2.4.1.1 0.72
-
glucose 1-phosphate chloroplast phosphorylase Pisum sativum
2.4.1.1 0.92
-
glucose 1-phosphate cytoplasmic phosphorylase Pisum sativum
2.4.1.1 4.1
-
phosphate chloroplast phosphorylase Pisum sativum
2.4.1.1 5.3
-
phosphate cytoplasmic phosphorylase Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.1 cytoplasm
-
Pisum sativum 5737
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Pisum sativum
-
Victory Freezer
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.1 2 isozymes, anion exchange, gel filtration, amylopectin-Sepharose affinity column Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 amylopectin + glucose 1-phosphate waxy rice or pea cotyledon Pisum sativum amylopectin + phosphate
-
?
2.4.1.1 amylose + phosphate pea cotyledon amylose Pisum sativum amylose + glucose 1-phosphate
-
?
2.4.1.1 glycogen + glucose 1-phosphate rabbit liver glycogen Pisum sativum glycogen + phosphate
-
?
2.4.1.1 glycogen + glucose 1-phosphate phytoglycogen Pisum sativum glycogen + phosphate
-
?
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
Pisum sativum [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
r