BRENDA - Enzyme Database
show all sequences of 1.5.5.2

Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate

Hancock, C.N.; Liu, W.; Alvord, W.G.; Phang, J.M.; Amino Acids 48, 859-872 (2016)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
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
Engineering
Protein Variants
Commentary
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
Commentary
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
Commentary
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
Commentary
Textmining
Homo sapiens
O43272
-
-
Mus musculus
Q9WU79
-
-
Purification (Commentary)
Purification (Commentary)
Organism
isolated mitochondria
Mus musculus
Synonyms
Synonyms
Commentary
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]
Commentary
Organism
37
-
assay at
Homo sapiens
37
-
assay at
Mus musculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Homo sapiens
7.2
-
assay at
Mus musculus
Cofactor
Cofactor
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
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
Engineering (protein specific)
Protein Variants
Commentary
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 (protein specific)
Inhibitors
Commentary
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 (protein specific)
Localization
Commentary
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
-
Purification (Commentary) (protein specific)
Commentary
Organism
isolated mitochondria
Mus musculus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
37
-
assay at
Mus musculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Homo sapiens
7.2
-
assay at
Mus musculus
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.5.5.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
7
43880
2017
-
-
1
1
1
-
-
3
-
-
-
2
-
6
-
-
-
-
-
-
4
-
4
1
1
1
-
-
3
1
-
-
3
-
-
-
-
-
1
3
1
1
-
-
-
-
3
-
-
-
2
-
-
-
-
-
-
4
-
4
1
1
-
-
3
1
-
-
-
-
-
-
-
3
3
741588
Hancock
Co-regulation of mitochondria ...
Homo sapiens, Mus musculus
Amino Acids
48
859-872
2016
-
-
2
-
1
-
12
-
2
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
4
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
1
-
-
12
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
6
6
-
-
-
741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
-
-
-
-
1
-
-
-
3
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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-
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-
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1
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-
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-
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3
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
6
-
-
-
2
2
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
2
-
-
-
-
-
-
-
1
1
2
2
1
-
-
742162
Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biotechnol. J.
10
395-403
2015
-
1
1
-
-
-
1
-
1
-
3
2
-
5
-
-
1
-
-
-
1
-
6
1
2
1
-
2
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
1
-
3
2
-
-
-
1
-
-
1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
-
-
-
-
-
-
2
-
2
-
-
1
-
4
-
-
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
-
2
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
2
2
1
-
-
724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
-
-
-
-
2
-
-
3
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
1
3
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
3
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus, Thermococcus profundus DSM 9503
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
-
-
4
-
-
-
8
-
-
-
-
-
-
13
-
-
4
-
-
-
-
-
22
7
24
4
-
4
-
4
-
-
4
-
-
-
-
-
7
7
-
-
-
-
14
-
-
-
-
-
-
-
-
-
7
-
-
-
-
22
7
7
-
7
-
7
-
-
-
-
8
14
-
-
-
742641
Omidinia
Expression, purification and ...
Pseudomonas putida, Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
2
2
3
1
1
-
-
1
1
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
2
1
1
-
-
1
1
-
-
-
1
1
-
-
-
743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
-
-
1
-
-
-
-
1
1
-
-
2
-
5
-
-
1
-
-
1
-
-
10
1
4
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
1
-
-
2
-
-
-
1
-
1
-
-
10
1
1
-
-
-
1
-
-
-
1
2
2
1
-
-
724345
Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
739932
Kawakami
L-proline dehydrogenases in hy ...
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Proline dehydrogenase activity ...
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Oxidation of L-thiazolidine-4- ...
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Redesigned purification yields ...
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Membrane association of prolin ...
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Membrane-bound proline dehydro ...
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