Cloned (Comment) | Organism |
---|---|
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K | Zea mays |
Protein Variants | Comment | Organism |
---|---|---|
R384A | mutation causes almost complete inactivation | Zea mays |
R384E | mutation causes almost complete inactivation | Zea mays |
R384K | residual activity of the mutant enzyme is 5% of the wild-type enzyme | Zea mays |
R384Q | mutation causes almost complete inactivation | Zea mays |
R384S | mutation causes almost complete inactivation | Zea mays |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0068 | - |
amylose | pH 7.5, 30°C, reduced amylose AS-320, wild-type enzyme | Zea mays | |
0.0113 | - |
amylose | pH 7.5, 30°C, reduced amylose AS-320, mutant enzyme R384K | Zea mays |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K | Zea mays |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
endosperm | - |
Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
amylose | - |
Zea mays | amylose containing alpha-1,6-glucosidic linkages | - |
? | |
additional information | the conserved Arg residue 384 plays an important role in the catalytic function but may not be directly involved in substrate binding | Zea mays | ? | - |
? |