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EC Number
General Information
Commentary
Reference
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
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; 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
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
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
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
metabolism
transcriptional induction of the enzyme causes changes in expression levels of other mitochondrial enzymes. Activities of the protein complexes of the respiratory chain were not significantly altered. But activity of glutamate dehydrogenase substantially increased, indicating upregulation of the entire proline catabolic pathway. Induction of D-lactate dehydrogenase activity allows rapid upregulation of ProDH activity during the short-term stress response in plants
more
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252
more
homology-based three-dimensional structural modeling of JcProDH, overview
more
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513
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
Results 1 - 10 of 18 > >>