EC Number   |
General Information |
Reference |
|---|
    1.5.5.2 | more |
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252 |
-, 742641 |
| 1.5.5.2 | physiological function |
endogenous ProDH2 expression is not able to overcome proline sensitivity of ProDH1 mutants, but overexpression of a GFP-tagged form of ProDH2 enables the utilisation of proline as single nitrogen source for growth |
711615 |
| 1.5.5.2 | more |
homology-based three-dimensional structural modeling of JcProDH, overview |
741642 |
| 1.5.5.2 | physiological function |
in trypanosomatids, L-proline is involved in a number of key processes, including energy metabolism, resistance to oxidative and nutritional stress and osmoregulation. In addition, this amino acid supports critical parasite life cycle processes by acting as an energy source, thus enabling host-cell invasion by the parasite and subsequent parasite differentiation. Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi, free proline accumulation constitutes a defense against oxidative imbalance |
-, 743635 |
| 1.5.5.2 | metabolism |
interdependent relationship between PRODH/POX, proline, and succinate and the regulation of respiration, detailed overview. Succinate dehydrogenae plays a specific role in the transmission of the PRODH/POX-generated reactive oxygen species signal. PRODH/POX-mediated ATP generation, overview |
741588 |
| 1.5.5.2 | more |
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513 |
-, 743635 |
| 1.5.5.2 | physiological function |
L-proline accumulates in many plant species in response to environmental stresses. Upon relief from stress, proline is rapidly oxidized in mitochondria by proline dehydrogenase (ProDH) and then by pyrroline-5-carboxylate dehydrogenase (P5CDH, EC 1.2.1.88). ProDH1 has a role in oxidizing excess proline and transferring electrons to the respiratory chain |
741858 |
| 1.5.5.2 | evolution |
nearly all of the residues responsible for the interaction with substrate and FAD are highly conserved in Pyrococcus and Thermococcus. Phylogenetic analysis shows that the divergence of the alphabetagammadelta-type PDHbetas is spread wider than that of alpha4beta4-type PDHbetas |
-, 741732 |
| 1.5.5.2 | metabolism |
proline dehydrogenase (ProDH) catalyzes the FAD-dependent oxidation of proline to DELTA1-pyrroline-5-carboxylate, the first step of proline catabolism in many organisms |
-, 742162 |
| 1.5.5.2 | physiological function |
proline dehydrogenase contributes to pathogen defense in Arabidopsis thaliana. The enzyme is a defense component contributing to hypersensitive response and disease resistance, which apparently potentiates the accumulation of relative oxygen species |
726218 |
