EC Number   |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Reference |
|---|
   3.5.1.117 | 9000 |
- |
1 * 27000 + 1 * 9000, SDS-PAGE |
728903 |
| 3.5.1.117 | 9000 |
- |
x * 27000 + x * 9000, SDS-PAGE |
684568 |
| 3.5.1.117 | 9000 |
- |
x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE |
718618 |
| 3.5.1.117 | 9513 |
- |
x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence |
718618 |
| 3.5.1.117 | 27000 |
- |
1 * 27000 + 1 * 9000, SDS-PAGE |
728903 |
| 3.5.1.117 | 27000 |
- |
4 * (1 * 27000 + 1 * 9000), four identical heterodimers (27 kDa + 9 kDa), which result from the autoprocessing of the precursor protein (36 kDa) constitute the doughnut-shaped quaternary structure, each heterodimer is folded into a single domain, generating a stacked alpha,beta,beta,alpha core structure |
720046 |
| 3.5.1.117 | 27000 |
- |
x * 27000 + x * 9000, SDS-PAGE |
684568 |
| 3.5.1.117 | 27408 |
- |
x * 27408 + x * 9513, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, calculation from nucleotide sequence |
718618 |
| 3.5.1.117 | 31000 |
- |
x * 31000 + x * 9000, the enzyme is made of two polypeptide chains arising from an internal cleavage between amino acid residues 266 and 267, SDS-PAGE |
718618 |
