EC Number   |
General Information |
Reference  |
|---|
    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 | 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 |
| 1.5.5.2 | malfunction |
treatment of cells with succinate inhibits production of PRODH/POX-dependent reactive oxygen species, mitigates inhibition of respiration by PRODH/POX, and restores protein levels of electron transport chain complexes in PRODH/POX-treated cells |
741588 |
| 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 | physiological function |
proline dehydrogenase/oxidase (PRODH/POX) is a mitochondrial protein critical to multiple stress pathways with roles in signaling, pleiotropic role of PRODH/POX in cellular energetics and signaling. PRODH/POX is a mediator of genotoxic, inflammatory, and metabolic stress signaling. Depending on cellular and environmental context, PRODH/POX can mediate programmed cell death, promote cell survival, or induce differentiation. Exposure of cells to PRODH/POX and proline results in a significant time and dependent decrease in total oxidative respiration due to PRODH/POX-dependent reactive oxygen species production. PRODH/POX has dose-dependent effect on the protein levels of individual subunits of Complexes I-IV of the electron transport chain, which is reversed with the PRODH/POX inhibitor 3,4-dehydro-L-proline and the antioxidant N-acetyl-L-cysteine |
741588 |
| 1.5.5.2 | more |
homology-based three-dimensional structural modeling of JcProDH, overview |
741642 |
| 1.5.5.2 | physiological function |
the JcProDH gene negatively participates in the stress response |
741642 |
| 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 | more |
values for kcat, Km, and Ki values for L-proline and Ki' for pyrrolidone-5-carboxylate differ greatly among the PDHbeta enzymes, which is in contrast to the optimal temperature and thermostability, and indicates that the kinetic parameters of the PDHbetas are not a reflection of whether the protein is a subunit of an alphabetagammadelta-type PDHbeta or alpha4beta4-type PDHbeta ProDH complex |
-, 741732 |
| 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 |
