EC Number |
Subunits |
Reference |
---|
3.5.2.9 | dimer |
- |
209374 |
3.5.2.9 | dimer |
2 * 140000, SDS-PAGE |
-, 209390, 209394, 712045 |
3.5.2.9 | dimer |
2 * 142000, SDS-PAGE |
209372, 209375, 209383, 209388 |
3.5.2.9 | More |
domain architecture, overview |
-, 756535 |
3.5.2.9 | More |
structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives |
-, 756017 |
3.5.2.9 | polymer |
2 protein compounds, component A exhibits 5-oxo-L-proline depedent ATPase activity, component A composed of 6 heterodimers, 6 * 51000 + 6 * 64000, SDS-PAGE, component B is a coupling protein without ATPase activity, 8 * 82000, octamer, SDS-PAGE |
209373 |
3.5.2.9 | polymer |
component A 1 * 65500 + 1 * 50000, component B 1 * 80000, SDS-PAGE |
209388 |
3.5.2.9 | tetramer |
4 * 115000, SDS-PAGE |
209375, 209383 |