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Literature summary for 1.5.5.2 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
Search for more literature for 1.5.5.2

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
2-Thenoyltrifluoroacetone an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity Homo sapiens
2-Thenoyltrifluoroacetone an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity Mus musculus
antimycin A very strong inhibition Homo sapiens
antimycin A very strong inhibition Mus musculus
KCN very strong inhibition Homo sapiens
KCN very strong inhibition Mus musculus
additional information no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II Homo sapiens
additional information no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II Mus musculus
rotenone an inhibitor of Complex I, addition of ROT only modestly affects PRODH/POX activity Homo sapiens
rotenone an inhibitor of Complex I, addition of ROT only modestly affects PRODH/POX activity Mus musculus
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
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

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

Organism

Organism UniProt Comment Textmining
Homo sapiens O43272
-
-
Mus musculus Q9WU79
-
-

Purification (Commentary)

Purification (Comment) Organism
isolated mitochondria Mus musculus

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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
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

General Information Comment Organism
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
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
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
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
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
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