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Literature summary for 2.4.1.1 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
Search for more literature for 2.4.1.1

Inhibitors

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

KM Value [mM]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
 Victory Freezer
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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