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Literature summary for 2.4.1.21 extracted from

  • MacDonald, F.D.; Preiss, J.
    Partial purification and characterization of granule-bound starch synthase from normal and waxy maize (1985), Plant Physiol., 78, 849-852.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information 0.002-1.5 mg/ml, value depends on isozyme and presence of citrate Zea mays
0.05
-
ADPglucose granule-bound isoenzyme II from waxy maize Zea mays
0.09
-
ADPglucose granule-bound isoenzyme I from waxy maize Zea mays
0.1 0.12 ADPglucose soluble isoenzymes Zea mays
0.11
-
ADPglucose granule-bound isoenzyme II Zea mays
0.14
-
ADPglucose granule-bound isoenzyme I Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Zea mays
-
-
starch grain
-
Zea mays 43036
-

Organism

Organism UniProt Comment Textmining
Zea mays
-
granule-bound isoenzymes I and II
-

Purification (Commentary)

Purification (Comment) Organism
6 isozymes Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-glucose + alpha-1,4-polyglucan granule-bound isoenzyme I shows higher activity with glycogen as primer than with amylopectin Zea mays ADP + alpha-1,4-polyglucan
-
?
ADP-glucose + alpha-1,4-polyglucan glucosyl acceptor: amylopectin Zea mays ADP + alpha-1,4-polyglucan
-
?