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

BRENDA support

Literature summary for 2.4.1.21 extracted from

  • Imparl-Radosevich, J.M.; Li, P.; Zhang, L.; McKean, A.L.; Keeling, P.L.; Guan, H.
    Purification and characterization of maize starch synthase I and its truncated forms (1998), Arch. Biochem. Biophys., 353, 64-72.
    View publication on PubMed
Search for more literature for 2.4.1.21

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli
expression of full-length and truncated enzyme in Escherichia coli Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli
additional information
-
 additional information recombinant starch synthase I, amylopectin: 0.24 mg/ml, glycogen: 0.041 mg/ml Zea mays
0.18
-
 ADPglucose starch synthase I, presence of 500 mM citrate Zea mays
0.24
-
 ADPglucose starch synthase I, absence of citrate Zea mays

Localization

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Zea mays
-
 starch synthase I
-

Purification (Commentary)

Purification (Comment) Organism
recombinant starch synthase I, ammonium sulfate, amylose column, Mono Q Zea mays

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.06
-
 unprimed reaction in the presence of 500 mM citrate, recombinant starch synthase I Zea mays
12.2
-
 primed reaction, recombinant starch synthase I Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40 50 recombinant starch synthase I in the presence of citrate Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 10.3 starch synthase II, sharp decline in activity below pH 7.0 Zea mays