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Information on EC 1.5.5.2 - proline dehydrogenase and Organism(s) Homo sapiens

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IUBMB Comments
A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor . In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate gamma-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
prodh, proline dehydrogenase, prodh/pox, prodh1, l-proline dehydrogenase, dye-linked l-proline dehydrogenase, puta flavoprotein, ttprodh, jcprodh, tcprodh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-proline dehydrogenase
-
-
-
-
PRODH/POX
-
proline dehydrogenase/oxidase
-
proline oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
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reduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-proline:quinone oxidoreductase
A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor [3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate gamma-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
9050-70-8
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Thenoyltrifluoroacetone
an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity
antimycin A
very strong inhibition
KCN
very strong inhibition
rotenone
an inhibitor of Complex I, addition of ROT only modestly affects PRODH/POX activity
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
additional information
no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
co-localization with the electron transport chain on the inner membrane of the mitochondria
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HYPDH_HUMAN
536
0
58871
Swiss-Prot
Mitochondrion (Reliability: 2)
PROD_HUMAN
600
0
68002
Swiss-Prot
Mitochondrion (Reliability: 3)
S4R3D8_HUMAN
73
0
8086
TrEMBL
other Location (Reliability: 4)
E7EQL6_HUMAN
492
0
56255
TrEMBL
other Location (Reliability: 2)
C9JIW4_HUMAN
135
0
15016
TrEMBL
other Location (Reliability: 1)
A0A590UKC3_HUMAN
460
0
50898
TrEMBL
Mitochondrion (Reliability: 4)
A0A481ZHW6_HUMAN
58
0
6566
TrEMBL
other Location (Reliability: 1)
A0A087WWM6_HUMAN
600
0
68029
TrEMBL
Mitochondrion (Reliability: 3)
K7EJK5_HUMAN
119
0
13195
TrEMBL
other Location (Reliability: 1)
X5D7N2_HUMAN
600
0
68002
TrEMBL
Mitochondrion (Reliability: 3)
A0A481ZII7_HUMAN
58
0
6580
TrEMBL
other Location (Reliability: 1)
H7C363_HUMAN
185
0
19200
TrEMBL
Mitochondrion (Reliability: 4)
O00420_HUMAN
826
1
90814
TrEMBL
Secretory Pathway (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene POX, stable recombinant expression in DLD-1 colorectal cancer cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hancock, C.N.; Liu, W.; Alvord, W.G.; Phang, J.M.
Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate
Amino Acids
48
859-872
2016
Homo sapiens (O43272), Mus musculus (Q9WU79)
Manually annotated by BRENDA team