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Literature summary extracted from

  • Hancock, C.N.; Liu, W.; Alvord, W.G.; Phang, J.M.
    Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate (2016), Amino Acids, 48, 859-872 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.5.2 gene POX, stable recombinant expression in DLD-1 colorectal cancer cells Homo sapiens
1.5.5.2 gene POX, stable recombinant expression in DLD-1 colorectal cancer cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
1.5.5.2 additional information expression of PRODH/POX in DLD-1 colorectal cancer cells significantly decreases basal and maximal respiration at both 3 and 5 days, and proline addition exacerbates this effect. PRODH/POX-dependent inhibition of respiration can be modulated by the duration of PRODH/POX expression and the availability of proline Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.5.2 2-Thenoyltrifluoroacetone an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity Homo sapiens
1.5.5.2 2-Thenoyltrifluoroacetone an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity Mus musculus
1.5.5.2 antimycin A very strong inhibition Homo sapiens
1.5.5.2 antimycin A very strong inhibition Mus musculus
1.5.5.2 KCN very strong inhibition Homo sapiens
1.5.5.2 KCN very strong inhibition Mus musculus
1.5.5.2 additional information no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II Homo sapiens
1.5.5.2 additional information no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II Mus musculus
1.5.5.2 rotenone an inhibitor of Complex I, addition of ROT only modestly affects PRODH/POX activity Homo sapiens
1.5.5.2 rotenone an inhibitor of Complex I, addition of ROT only modestly affects PRODH/POX activity Mus musculus
1.5.5.2 succinate uncompetitive inhibitor, in the presence of low levels of proline in vivo, higher levels of succinate can act to inhibit PRODH/POX activity and reactive oxygena species generation. The affinity of succinate is for the enzyme-substrate complex of PRODH/POX and proline rather than for the enzyme binding site for proline. Succinate protects electron transport chain component proteins from PRODH/POX reactive oxygen species-mediated downregulation with almost the same efficacy as 3,4-dehydro-L-proline and N-acetyl-L-cysteine Homo sapiens
1.5.5.2 succinate uncompetitive inhibitor, in the presence of low levels of proline in vivo, higher levels of succinate can act to inhibit PRODH/POX activity and reactive oxygena species generation. The affinity of succinate is for the enzyme-substrate complex of PRODH/POX and proline rather than for the enzyme binding site for proline. Succinate protects electron transport chain component proteins from PRODH/POX reactive oxygen species-mediated downregulation with almost the same efficacy as 3,4-dehydro-L-proline and N-acetyl-L-cysteine Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.5.2 mitochondrial inner membrane co-localization with the electron transport chain on the inner membrane of the mitochondria Homo sapiens 5743
-
1.5.5.2 mitochondrial inner membrane co-localization with the electron transport chain on the inner membrane of the mitochondria Mus musculus 5743
-

Organism

EC Number Organism UniProt Comment Textmining
1.5.5.2 Homo sapiens O43272
-
-
1.5.5.2 Mus musculus Q9WU79
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.5.2 isolated mitochondria Mus musculus

Synonyms

EC Number Synonyms Comment Organism
1.5.5.2 PRODH/POX
-
 Homo sapiens
1.5.5.2 PRODH/POX
-
 Mus musculus
1.5.5.2 proline dehydrogenase/oxidase
-
 Homo sapiens
1.5.5.2 proline dehydrogenase/oxidase
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.5.2 37
-
 assay at Homo sapiens
1.5.5.2 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.5.2 7.2
-
 assay at Homo sapiens
1.5.5.2 7.2
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.5.2 coenzyme Q1 coenzyme Q1 is electron acceptor for PRODH/POX, which passes electrons directly to coenzyme Q1 (CoQ1) RODH/POX binds directly to CoQ1 without the formation of a tertiary complex. The transfer of electrons from proline to CoQ1 by PRODH/POX is dependent on downstream electron transfer from CoQ1 to Complexes III and IV Homo sapiens
1.5.5.2 coenzyme Q1 coenzyme Q1 is electron acceptor for PRODH/POX, which passes electrons directly to coenzyme Q1 (CoQ1) RODH/POX binds directly to CoQ1 without the formation of a tertiary complex. The transfer of electrons from proline to CoQ1 by PRODH/POX is dependent on downstream electron transfer from CoQ1 to Complexes III and IV Mus musculus

General Information

EC Number General Information Comment Organism
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 Homo sapiens
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 Mus musculus
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 Homo sapiens
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 Mus musculus
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 Homo sapiens
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 Mus musculus