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Literature summary for 2.4.1.21 extracted from

  • Cao, H.; James, M.G.; Myers, A.M.
    Purification and characterization of soluble starch synthases from maize endosperm (2000), Arch. Biochem. Biophys., 373, 135-146.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information starch synthase I, amylopectin: 0.08 mg/ml in the presence of citrate, 0.13 mg/ml in the absence of citrate, glycogen: 0.043 mg/ml in the presence of citrate, 12.8 mg/ml in the absence of citrate Zea mays
0.053
-
ADPglucose starch synthase I, primer amylopectin Zea mays
0.11
-
ADPglucose starch synthase I, primer amylopectin, 500 mM citrate Zea mays
0.3
-
ADPglucose starch synthase II, primer amylopectin, 500 mM citrate Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
starch synthase II
-

Purification (Commentary)

Purification (Comment) Organism
starch synthases I and II, Q-Sepharose, Mono Q, amylose-agarose Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm starch synthase I and II Zea mays
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
starch synthase II, 60% of maximal activity at 23°C Zea mays
42
-
starch synthase I, 15% of maximal activity at 23°C Zea mays

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
starch synthase I, no loss of activity after 30 min, starch synthase II, loss of more than 50% activity after 30 min Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
starch synthase II, 75% of maximal activity at pH 6.5 Zea mays
8
-
starch synthase I, 34% of maximal activity at pH 6.5 Zea mays