Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant AGPases in Escherichia coli strain AC70R1-504, wild-type BT2 and mutant BT2-TI show very low expression levels, overview | Zea mays |
Protein Variants | Comment | Organism |
---|---|---|
additional information | heat-stable small subunit variant MP is composed of sequences from the maize endosperm and the potato tuber small subunit, construction of a double mutant MP-TI, which may lead to increased starch yield when expressed in monocot endosperms | Zea mays |
T462I | random mutagenesis, small subunit mutant BT2-TI, BT2-TI exhibits enhanced heat stability compared to wildtype maize endosperm AGPase | Zea mays |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | recombinant wild-type and mutant AGPase kinetic and allosteric properties for the forward and reverse reaction directions, overview | Zea mays | |
0.04 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, mutant BT2-TI | Zea mays | |
0.05 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, wild-type BT2 | Zea mays | |
0.06 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, mutant MP-TI | Zea mays | |
0.07 | - |
ADP-D-glucose | pH 7.4, 37°C, mutant MP-TI | Zea mays | |
0.08 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, mutant MP | Zea mays | |
0.11 | - |
ADP-D-glucose | pH 7.4, 37°C, mutant MP | Zea mays | |
0.11 | - |
ATP | pH 7.4, 37°C, wild-type BT2 and mutant MP-TI | Zea mays | |
0.13 | - |
ATP | pH 7.4, 37°C, mutant MP | Zea mays | |
0.15 | - |
ATP | pH 7.4, 37°C, mutant BT2-TI | Zea mays | |
0.33 | - |
ADP-D-glucose | pH 7.4, 37°C, mutant BT2-TI | Zea mays | |
0.48 | - |
ADP-D-glucose | pH 7.4, 37°C, wild-type BT2 | Zea mays | |
2.32 | - |
diphosphate | pH 7.4, 37°C, wild-type BT2 | Zea mays | |
4.07 | - |
diphosphate | pH 7.4, 37°C, mutant BT2-TI | Zea mays | |
5.87 | - |
diphosphate | pH 7.4, 37°C, mutant MP-TI | Zea mays | |
6.61 | - |
diphosphate | pH 7.4, 37°C, mutant MP | Zea mays |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Zea mays |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | Zea mays | - |
ADP-D-glucose + diphosphate | - |
r | |
additional information | Zea mays | ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
endosperm | - |
Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + alpha-D-glucose 1-phosphate | - |
Zea mays | ADP-D-glucose + diphosphate | - |
r | |
additional information | ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview | Zea mays | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the three-dimensional monomer structures of the mutants AGPases BT2, BT2-TI, MP and MP-TI are modeled after the potato small subunit, overview | Zea mays |
Synonyms | Comment | Organism |
---|---|---|
ADP-glucose pyrophosphorylase | - |
Zea mays |
AGPase | - |
Zea mays |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Zea mays |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
42 | - |
half-lives of wild-type and mutant enzymes lay between 2 and 17 min, overview | Zea mays |
53 | - |
half-lives of wild-type and mutant enzymes lay between 2 and 16 min, overview | Zea mays |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
26.21 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, mutant BT2-TI | Zea mays | |
29.11 | - |
ATP | pH 7.4, 37°C, mutant BT2-TI | Zea mays | |
38.17 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, wild-type BT2 | Zea mays | |
42.88 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, mutant MP-TI | Zea mays | |
43.32 | - |
ATP | pH 7.4, 37°C, wild-type BT2 | Zea mays | |
49.03 | - |
ATP | pH 7.4, 37°C, mutant MP-TI | Zea mays | |
62.65 | - |
alpha-D-glucose 1-phosphate | pH 7.4, 37°C, mutant MP | Zea mays | |
69.34 | - |
ATP | pH 7.4, 37°C, mutant MP | Zea mays |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Zea mays |