Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydroxy-L-proline + acceptor + H2O
?
-
3%5 the rate of L-proline
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
L-proline + cytochrome c
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
L-proline + FAD + H2O
(S)-1-pyrroline-5-carboxylate + FADH2
-
-
-
-
?
L-proline + ferricyanide + H2O
(S)-1-pyrroline-5-carboxylate + ferrocyanide
-
-
-
?
L-proline + NAD+
(S)-1-pyrroline-5-carboxylate + NADH
L-proline + NAD+ + H2O
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
L-proline + oxidized dichlorophenolindophenol
1-pyrroline-5-carboxylate + reduced dichlorophenolindophenol
-
-
-
?
L-proline + oxidized phenazine methosulfate
(S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate
-
-
-
-
?
L-thiazolidine-4-carboxylate + acceptor + H2O
N-formylcysteine + reduced acceptor
-
-
-
?
trans-4-hydroxy-L-proline + oxidized dichlorophenolindophenol
?
-
-
-
?
additional information
?
-
L-proline + 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
+ phenazine methosulfate as mediator
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
-
-
ir
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
a FAD-dependent reaction
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
a FAD-dependent reaction
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
-
-
ir
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
-
-
ir
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
-
-
ir
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
-
-
?
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
enzyme exists in soluble and in membrane associated forms differing in catalytic properties
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
PutA flavoprotein plays multiple roles in proline catabolism by functioning as a membrane-associated bi-functional enzyme and a transcriptional repressor of proline utilization genes
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
the enzyme catalyzes the first step of proline catabolism
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
-
?
L-proline + cytochrome c
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
-
-
ir
L-proline + cytochrome c
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2
-
-
ir
L-proline + NAD+
(S)-1-pyrroline-5-carboxylate + NADH
NADP+ is a poor electron acceptor
-
-
?
L-proline + NAD+
(S)-1-pyrroline-5-carboxylate + NADH
NADP+ is a poor electron acceptor
-
-
?
additional information
?
-
-
no substrate: D-proline, other L-amino acids, L-azetidine-2-carboxylate, succinate
-
-
?
additional information
?
-
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
-
-
?
additional information
?
-
-
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
-
-
?
additional information
?
-
the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier
-
-
?
additional information
?
-
-
the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier
-
-
?
additional information
?
-
the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier
-
-
?
additional information
?
-
-
the enzyme is assayed with L-proline as substrate and 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) as a terminal electron acceptor and phenazine methosulfate (PMS) as a mediator electron carrier
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
no activity with D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine
-
-
?
additional information
?
-
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
-
-
?
additional information
?
-
-
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
-
-
?
additional information
?
-
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-Thenoyltrifluoroacetone
5-ethylpentyl-barbituric acid
-
membrane-associated enzyme, not soluble enzyme
cyanide
-
only membrane-associated enzyme, not soluble enzyme
GuHCl
enzyme unfolding at 1 M, 0.5 M is not enough for proper unfolding. The fusion protein forms visible aggregates due to unfolding of MBP
L-azetidine-2-carboxylate
-
competitive
L-tetrahydro-2-furoic acid
L-thiazolidine-4-carboxylate
-
competitive
N-propargylglycine
irreversibly inactivates PutA by covalently linking the flavin N(5) atom to the epsilon-amino of Lys329. Inactivation locks PutA into a conformation that may mimic the proline-reduced, membrane-associated form
pyrrolidone-5-carboxylate
thiazolidine-2-carboxylate
a mechanism-based inactivator of PRODH. PRODH catalyzes the oxidation of thiazolidine-2-carboxylate at the C atom adjacent to the S atom of the thiazolidine ring (C5). Then, the N5 atom of the reduced FAD attacks the C5 of the oxidized T2C species, resulting in a covalent adduct
2-Thenoyltrifluoroacetone
an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity
2-Thenoyltrifluoroacetone
an inhibitor of Complex II, addition of TTFA significantly reduces PRODH/POX activity
antimycin A
very strong inhibition
antimycin A
very strong inhibition
D-lactate
-
a competitive inhibitor of ProDH in plants
KCN
very strong inhibition
KCN
very strong inhibition
L-lactate
-
a competitive inhibitor of ProDH in plants
L-proline
substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations
L-proline
substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations
L-proline
substrate inhibition at high L-proline concentrations; substrate inhibition at high L-proline concentrations
L-proline
substrate inhibition at high L-proline concentrations
L-tetrahydro-2-furoic acid
competitive
L-tetrahydro-2-furoic acid
-
pyrrolidone-5-carboxylate
-
pyrrolidone-5-carboxylate
-
pyrrolidone-5-carboxylate
-
pyrrolidone-5-carboxylate
-
rotenone
an inhibitor of Complex I, addition of ROT only modestly affects PRODH/POX activity
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
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
-
additional information
no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
22q11 Deletion Syndrome
Functional polymorphisms in PRODH are associated with risk and protection for schizophrenia and fronto-striatal structure and function.
22q11 Deletion Syndrome
PRODH rs450046 and proline x COMT Val¹?? Met interaction effects on intelligence and startle in adults with 22q11 deletion syndrome.
Brain Neoplasms
N-Propargylglycine: a unique suicide inhibitor of proline dehydrogenase with anticancer activity and brain-enhancing mitohormesis properties.
Breast Neoplasms
Functional Consequences of Intracellular Proline Levels Manipulation Affecting PRODH/POX-Dependent Pro-Apoptotic Pathways in a Novel in Vitro Cell Culture Model.
Breast Neoplasms
HDAC inhibitors induce proline dehydrogenase (POX) transcription and anti-apoptotic autophagy in triple negative breast cancer.
Breast Neoplasms
Proline metabolism supports metastasis formation and could be inhibited to selectively target metastasizing cancer cells.
Breast Neoplasms
Proline oxidase silencing induces proline-dependent pro-survival pathways in MCF-7 cells.
Breast Neoplasms
Sources of superoxide/H2O2 during mitochondrial proline oxidation.
Breast Neoplasms
Targeting Mitochondrial Proline Dehydrogenase with a Suicide Inhibitor to Exploit Synthetic Lethal Interactions with p53 Upregulation and Glutaminase Inhibition.
Carcinogenesis
Cancer progression is mediated by proline catabolism in non-small cell lung cancer.
Carcinogenesis
HDAC inhibitors induce proline dehydrogenase (POX) transcription and anti-apoptotic autophagy in triple negative breast cancer.
Carcinogenesis
Proline dehydrogenase (oxidase) in cancer.
Carcinoma
Proline dehydrogenase is essential for proline protection against hydrogen peroxide-induced cell death.
Catatonia
Medical and developmental risk factors of catatonia in children and adolescents: A prospective case-control study.
Coma
Medical and developmental risk factors of catatonia in children and adolescents: A prospective case-control study.
Dehydration
A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis.
Dehydration
ACTCAT, a novel cis-acting element for proline- and hypoosmolarity-responsive expression of the ProDH gene encoding proline dehydrogenase in Arabidopsis.
Dehydration
Effect of Exogenous Abscisic Acid on Proline Dehydrogenase Activity in Maize (Zea mays L.).
Dehydration
Effect of water stress on growth and proline metabolism of Phaseolus vulgaris L.
Dehydration
Expression analysis of proline metabolism-related genes from halophyte Arabis stelleri under osmotic stress conditions.
Dehydration
Proline metabolic dynamics and implications in drought tolerance of peanut plants.
Dehydration
Regulation of levels of proline as an osmolyte in plants under water stress.
DiGeorge Syndrome
Association of COMT and PRODH gene variants with intelligence quotient (IQ) and executive functions in 22q11.2DS subjects.
DiGeorge Syndrome
Early neurological phenotype in 4 children with biallelic PRODH mutations.
DiGeorge Syndrome
Hyperprolinemia is a risk factor for schizoaffective disorder.
DiGeorge Syndrome
Schizophrenia-like neurophysiological abnormalities in 22q11.2 deletion syndrome and their association to COMT and PRODH genotypes.
DiGeorge Syndrome
The 22q11 PRODH/DGCR6 deletion is frequent in hyperprolinemic subjects but is not a strong risk factor for ASD.
Encephalitis
Medical and developmental risk factors of catatonia in children and adolescents: A prospective case-control study.
Epilepsy
Type I hyperprolinemia and proline dehydrogenase (PRODH) mutations in four Italian children with epilepsy and mental retardation.
Heart Failure
Exercise Reveals Proline Dehydrogenase as a Potential Target in Heart Failure.
Hypersensitivity
Altered levels of proline dehydrogenase cause hypersensitivity to proline and its analogs in Arabidopsis.
Infections
Differential control and function of Arabidopsis ProDH1 and ProDH2 genes upon infection with biotrophic and necrotrophic pathogens.
Infections
P5CDH affects the pathways contributing to Pro synthesis after ProDH activation by biotic and abiotic stress conditions.
Insomnia, Fatal Familial
Medical and developmental risk factors of catatonia in children and adolescents: A prospective case-control study.
Intellectual Disability
Type I hyperprolinemia and proline dehydrogenase (PRODH) mutations in four Italian children with epilepsy and mental retardation.
Liver Neoplasms
Reprogramming of mitochondrial proline metabolism promotes liver tumorigenesis.
Mouth Neoplasms
Proline-Dependent Induction of Apoptosis in Oral Squamous Cell Carcinoma (OSCC)-The Effect of Celecoxib.
Myocardial Infarction
Metabolomic Analysis of the Ameliorative Effect of Enhanced Proline Metabolism on Hypoxia-Induced Injury in Cardiomyocytes.
Neoplasm Metastasis
Proline dehydrogenase in cancer: apoptosis, autophagy, nutrient dependency and cancer therapy.
Neoplasm Metastasis
Proline metabolism supports metastasis formation and could be inhibited to selectively target metastasizing cancer cells.
Neoplasms
1-Pyrroline-5-carboxylate released by prostate Cancer cell inhibit T cell proliferation and function by targeting SHP1/cytochrome c oxidoreductase/ROS Axis.
Neoplasms
Cancer progression is mediated by proline catabolism in non-small cell lung cancer.
Neoplasms
Collagen metabolism as a regulator of proline dehydrogenase/proline oxidase-dependent apoptosis/autophagy.
Neoplasms
Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate.
Neoplasms
Expression signatures in lung cancer reveal a profile for EGFR-mutant tumours and identify selective PIK3CA overexpression by gene amplification.
Neoplasms
In search of druggable targets for GBM amino acid metabolism.
Neoplasms
N-Propargylglycine: a unique suicide inhibitor of proline dehydrogenase with anticancer activity and brain-enhancing mitohormesis properties.
Neoplasms
Oncogenic human herpesvirus hijacks proline metabolism for tumorigenesis.
Neoplasms
P53 family members modulate the expression of PRODH, but not PRODH2, via intronic p53 response elements.
Neoplasms
Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles.
Neoplasms
Prolidase-proline dehydrogenase/proline oxidase-collagen biosynthesis axis as a potential interface of apoptosis/autophagy.
Neoplasms
Proline dehydrogenase (oxidase) in cancer.
Neoplasms
Proline dehydrogenase (oxidase), a mitochondrial tumor suppressor, and autophagy under the hypoxia microenvironment.
Neoplasms
Proline dehydrogenase in cancer: apoptosis, autophagy, nutrient dependency and cancer therapy.
Neoplasms
Proline dehydrogenase is essential for proline protection against hydrogen peroxide-induced cell death.
Neoplasms
Proline metabolism and cancer.
Neoplasms
Proline metabolism supports metastasis formation and could be inhibited to selectively target metastasizing cancer cells.
Neoplasms
Reprogramming of proline and glutamine metabolism contributes to the proliferative and metabolic responses regulated by oncogenic transcription factor c-MYC.
Neoplasms
Role of apoptosis-inducing factor, proline dehydrogenase, and NADPH oxidase in apoptosis and oxidative stress.
Neoplasms
Sources of superoxide/H2O2 during mitochondrial proline oxidation.
Neoplasms
Structure, biochemistry, and gene expression patterns of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase (PYCR), an emerging cancer therapy target.
Neoplasms
Targeting Mitochondrial Proline Dehydrogenase with a Suicide Inhibitor to Exploit Synthetic Lethal Interactions with p53 Upregulation and Glutaminase Inhibition.
Neoplasms
The Janus-like role of proline metabolism in cancer.
Neoplasms
The Proline Cycle As a Potential Cancer Therapy Target.
Nervous System Diseases
Human-specific endogenous retroviral insert serves as an enhancer for the schizophrenia-linked gene PRODH.
Neurologic Manifestations
PRODH mutations and hyperprolinemia in a subset of schizophrenic patients.
proline dehydrogenase deficiency
Mitochondrial proline dehydrogenase deficiency in hyperprolinemic PRO/Re mice: genetic and enzymatic analyses.
proline dehydrogenase deficiency
Transcriptional and behavioral interaction between 22q11.2 orthologs modulates schizophrenia-related phenotypes in mice.
pyrroline-5-carboxylate reductase deficiency
Identification of PRODH Mutations in Korean Neonates with Type I Hyperprolinemia.
Seizures
Medical and developmental risk factors of catatonia in children and adolescents: A prospective case-control study.
Sleep Initiation and Maintenance Disorders
Medical and developmental risk factors of catatonia in children and adolescents: A prospective case-control study.
Starvation
Heterodimers of the Arabidopsis Transcription Factors bZIP1 and bZIP53 Reprogram Amino Acid Metabolism during Low Energy Stress.
Triple Negative Breast Neoplasms
HDAC inhibitors induce proline dehydrogenase (POX) transcription and anti-apoptotic autophagy in triple negative breast cancer.
Tuberculosis
Kinetic and Isotopic Characterization of l-Proline Dehydrogenase from Mycobacterium tuberculosis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
21.9 - 79.5
2,6-dichlorophenolindophenol
1.438 - 90.32
coenzyme Q1
0.125
L-hydroxyproline
-
in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
21.9
2,6-dichlorophenolindophenol
-
with L-hydroxyproline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
79.5
2,6-dichlorophenolindophenol
-
with L-proline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
1.438
coenzyme Q1
-
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
1.535
coenzyme Q1
-
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
90.32
coenzyme Q1
-
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.00021
L-proline
-
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.0011
L-proline
-
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.03
L-proline
-
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.117
L-proline
-
mutant enzyme Y203F, at 25°C and pH 7.1 in 20 mM Tris-HCl
0.124
L-proline
pH 7.5, 21°C
1.25
L-proline
-
in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
1.78
L-proline
-
TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
4.31
L-proline
-
PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
5.67
L-proline
-
PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
5.87
L-proline
-
PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
5.877
L-proline
-
wild type enzyme, at 25°C and pH 7.1 in 20 mM Tris-HCl
7.95
L-proline
-
TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
11.3
L-proline
-
TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
11.6
L-proline
-
TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
20.1
L-proline
-
PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
146
L-proline
recombinant holo-enzyme, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
158
L-proline
recombinant apo-enzyme reconstituted with FMN, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
198
L-proline
recombinant apo-enzyme reconstituted with FAD, pH 7.4, 25°C, with 2,6-dichlorphenol-indophenol
31
NAD+
overall reaction of bifunctional enzyme, pH 7.5, 21°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
-
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
-
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
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
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
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
-
physiological function
-
endogenous ProDH2 expression is not able to overcome proline sensitivity of ProDH1 mutants, but overexpression of a GFP-tagged form of ProDH2 enables the utilisation of proline as single nitrogen source for growth
physiological function
-
proline dehydrogenase contributes to pathogen defense in Arabidopsis thaliana. The enzyme is a defense component contributing to hypersensitive response and disease resistance, which apparently potentiates the accumulation of relative oxygen species
physiological function
in trypanosomatids, L-proline is involved in a number of key processes, including energy metabolism, resistance to oxidative and nutritional stress and osmoregulation. In addition, this amino acid supports critical parasite life cycle processes by acting as an energy source, thus enabling host-cell invasion by the parasite and subsequent parasite differentiation. Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi, free proline accumulation constitutes a defense against oxidative imbalance
physiological function
L-proline accumulates in many plant species in response to environmental stresses. Upon relief from stress, proline is rapidly oxidized in mitochondria by proline dehydrogenase (ProDH) and then by pyrroline-5-carboxylate dehydrogenase (P5CDH, EC 1.2.1.88). ProDH1 has a role in oxidizing excess proline and transferring electrons to the respiratory chain
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
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
physiological function
the JcProDH gene negatively participates in the stress response
physiological function
-
transcriptional induction of the enzyme causes changes in expression levels of other mitochondrial enzymes. Activity of glutamate dehydrogenase substantially increased, indicating upregulation of the entire proline catabolic pathway
physiological function
-
in trypanosomatids, L-proline is involved in a number of key processes, including energy metabolism, resistance to oxidative and nutritional stress and osmoregulation. In addition, this amino acid supports critical parasite life cycle processes by acting as an energy source, thus enabling host-cell invasion by the parasite and subsequent parasite differentiation. Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi, free proline accumulation constitutes a defense against oxidative imbalance
-
additional information
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252
additional information
-
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252
additional information
homology-based three-dimensional structural modeling of JcProDH, overview
additional information
-
homology-based three-dimensional structural modeling of JcProDH, overview
additional information
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513
additional information
-
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513
additional information
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
additional information
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
additional information
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
additional information
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
additional information
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
additional information
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
additional information
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
additional information
-
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
-
additional information
-
key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513
-
additional information
-
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
-
additional information
-
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252
-
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterooctamer
4 * 55300 + 4 * 42700, calculated from amino acid sequence
homodimer
-
2 * 37000, SDS-PAGE
?
-
x * 55000-57000, SDS-PAGE
?
x * 54000, about, sequence calculation
?
x * 40000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 40000, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
-
2 * 119000-124000, SDS-PAGE
dimer
domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a beta/alpha-barrel PRODH domain with a bound lactate inhibitor
dimer
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE
dimer
2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation
dimer
-
2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation
-
octamer
the enzyme is a alpha4beta4-type ProDH
octamer
the enzyme is a alpha4beta4-type ProDH
octamer
-
the enzyme is a alpha4beta4-type ProDH
-
octamer
the enzyme is a alpha4beta4-type ProDH
octamer
-
the enzyme is a alpha4beta4-type ProDH
-
tetramer
the enzyme is a alphabetagammadelta-type ProDH
tetramer
the enzyme is a alphabetagammadelta-type ProDH
tetramer
-
the enzyme is a alphabetagammadelta-type ProDH
-
tetramer
the enzyme is a alphabetagammadelta-type ProDH
tetramer
-
alpha,beta, 2 * 50000 + 2 * 40000, SDS-PAGE
tetramer
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE
tetramer
the enzyme is a alphabetagammadelta-type ProDH
tetramer
-
the enzyme is a alphabetagammadelta-type ProDH
-
additional information
homology-based three-dimensional structural modeling of JcProDH, overview
additional information
-
homology-based three-dimensional structural modeling of JcProDH, overview
additional information
Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview
additional information
-
Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview
additional information
-
Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview
-
additional information
recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
additional information
-
recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
additional information
-
recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Wood, J.M.
Membrane association of proline dehydrogenase in Escherichia coli is redox dependent
Proc. Natl. Acad. Sci. USA
84
373-377
1987
Escherichia coli
brenda
Graham, S.B.; Stephenson, J.T.; Wood, J.M.
Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association
J. Biol. Chem.
259
2656-2661
1984
Escherichia coli
brenda
Scarpulla, R.C.; Soffer, R.L.
Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization
J. Biol. Chem.
253
5997-6001
1978
Escherichia coli
brenda
Nadaraia, S.; Lee, Y.H.; Becker, D.F.; Tanner, J.J.
Crystallization and preliminary crystallographic analysis of the proline dehydrogenase domain of the multifunctional PutA flavoprotein from Escherichia coli
Acta Crystallogr. Sect. D
57
1925-1927
2001
Escherichia coli
brenda
Deutch, C.E.
Oxidation of L-thiazolidine-4-carboxylate by L-proline dehydrogenase in Escherichia coli
J. Gen. Microbiol.
138
1593-1598
1992
Escherichia coli
-
brenda
Sakuraba, H.; Takamatsu, Y.; Satomura, T.; Kawakami, R.; Ohshima, T.
Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus
Appl. Environ. Microbiol.
67
1470-1475
2001
Thermococcus profundus
brenda
Brown, E.D.; Wood, J.M.
Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline
J. Biol. Chem.
268
8972-8979
1993
Escherichia coli
brenda
Chaudhary, S.; Dudeja, S.S.; Sharma, H.R.; Khurana, A.L.; Malik, M.S.
Proline dehydrogenase activity of mungbean rhizobia and their proline prototrophs in relation to their efficacy in symbiotic association
Indian J. Exp. Biol.
37
1234-1240
1999
Vigna radiata
-
brenda
Zhang, M.; White, T.A.; Schuermann, J.P.; Baban, B.A.; Becker, D.F.; Tanner, J.J.
Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors
Biochemistry
43
12539-12548
2004
Escherichia coli (P09546), Escherichia coli
brenda
Baban, B.A.; Vinod, M.P.; Tanner, J.J.; Becker, D.F.
Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA
Biochim. Biophys. Acta
1701
49-59
2004
Escherichia coli
brenda
Kawakami, R.; Sakuraba, H.; Ohshima, T.
Gene and primary structures of dye-linked L-proline dehydrogenase from the hyperthermophilic archaeon Thermococcus profundus show the presence of a novel heterotetrameric amino acid dehydrogenase complex
Extremophiles
8
99-108
2004
Thermococcus profundus (Q76M73), Thermococcus profundus (Q76M76), Thermococcus profundus
brenda
Lee, Y.H.; Nadaraia, S.; Gu, D.; Becker, D.F.; Tanner, J.J.
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
Nat. Struct. Biol.
10
109-114
2003
Escherichia coli (P09546), Escherichia coli
brenda
Zhu, W.; Becker, D.F.
Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy
Biochemistry
44
12297-12306
2005
Escherichia coli
brenda
Ostrander, E.L.; Larson, J.D.; Schuermann, J.P.; Tanner, J.J.
A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate
Biochemistry
48
951-959
2009
Escherichia coli (P09546), Escherichia coli
brenda
Srivastava, D.; Zhu, W.; Johnson, W.H.; Whitman, C.P.; Becker, D.F.; Tanner, J.J.
The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction
Biochemistry
49
560-569
2010
Escherichia coli (P09546), Escherichia coli
brenda
Brown, E.D.; Wood, J.M.
Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli
J. Biol. Chem.
267
13086-13092
1992
Escherichia coli (P09546), Escherichia coli
brenda
Moxley, M.A.; Becker, D.F.
Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein
Biochemistry
51
511-520
2012
Escherichia coli
brenda
Serrano, H.; Blanchard, J.S.
Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
Mycobacterium tuberculosis
brenda
Kawakami, R.; Satomura, T.; Sakuraba, H.; Ohshima, T.
L-proline dehydrogenases in hyperthermophilic archaea: distribution, function, structure, and application
Appl. Microbiol. Biotechnol.
93
83-93
2012
Pyrococcus horikoshii (O59088 and O59089)
brenda
Moxley, M.A.; Sanyal, N.; Krishnan, N.; Tanner, J.J.; Becker, D.F.
Evidence for hysteretic substrate channeling in the proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA)
J. Biol. Chem.
289
3639-3651
2014
Escherichia coli (P09546), Escherichia coli
brenda
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)
brenda
Wang, H.; Ao, P.; Yang, S.; Zou, Z.; Wang, S.; Gong, M.
Molecular cloning and expression analysis of the gene encoding proline dehydrogenase from Jatropha curcas L
Appl. Biochem. Biotechnol.
175
2413-2426
2015
Jatropha curcas (V9XZ65), Jatropha curcas
brenda
Kawakami, R.; Noguchi, C.; Higashi, M.; Sakuraba, H.; Ohshima, T.
Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
Pyrococcus horikoshii (O59089), Pyrococcus horikoshii (O59445), Thermococcus kodakarensis (Q5JFG2), Thermococcus kodakarensis (Q5JFG7), Thermococcus profundus (Q76M73), Pyrococcus furiosus (Q8U022), Pyrococcus furiosus (Q8U1G2), Thermococcus kodakarensis KOD1 JCM12380 (Q5JFG7), Thermococcus profundus DSM 9503 (Q76M73), Pyrococcus horikoshii OT-3 (O59089), Pyrococcus horikoshii OT-3 (O59445)
brenda
Cabassa-Hourton, C.; Schertl, P.; Bordenave-Jacquemin, M.; Saadallah, K.; Guivarch, A.; Lebreton, S.; Planchais, S.; Klodmann, J.; Eubel, H.; Crilat, E.; Lefebvre-De Vos, D.; Ghelis, T.; Richard, L.; Abdelly, C.; Carol, P.; Braun, H.P.; Savoure, A.
Proteomic and functional analysis of proline dehydrogenase 1 link proline catabolism to mitochondrial electron transport in Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
Arabidopsis thaliana (P92983), Arabidopsis thaliana
brenda
Huijbers, M.M.; van Berkel, W.J.
High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag
Biotechnol. J.
10
395-403
2015
Thermus thermophilus (Q72IB8), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72IB8)
brenda
Schertl, P.; Cabassa, C.; Saadallah, K.; Bordenave, M.; Savoure, A.; Braun, H.P.
Biochemical characterization of proline dehydrogenase in Arabidopsis mitochondria
FEBS J.
281
2794-2804
2014
Arabidopsis thaliana
brenda
Omidinia, E.; Mahdizadehdehosta, R.; Mohammadi, H.S.
Expression, purification and characterization of the proline dehydrogenase domain of PutA from Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
Pseudomonas putida (I2D0K8), Pseudomonas putida, Pseudomonas putida POS-F84 (I2D0K8), Pseudomonas putida POS-F84
brenda
Paes, L.S.; Suarez Mantilla, B.; Zimbres, F.M.; Pral, E.M.; Diogo de Melo, P.; Tahara, E.B.; Kowaltowski, A.J.; Elias, M.C.; Silber, A.M.
Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi
PLoS ONE
8
e69419
2013
Trypanosoma cruzi (Q4CVA1), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4CVA1)
brenda
Huijbers, M.M.; Martinez-Julvez, M.; Westphal, A.H.; Delgado-Arciniega, E.; Medina, M.; van Berkel, W.J.
Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor
Sci. Rep.
7
43880
2017
Thermus thermophilus (Q72IB8), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72IB8)
brenda
Campbell, A.C.; Becker, D.F.; Gates, K.S.; Tanner, J.J.
Covalent modification of the flavin in proline dehydrogenase by thiazolidine-2-carboxylate
ACS Chem. Biol.
15
936-944
2020
Sinorhizobium meliloti (F7X6I3), Sinorhizobium meliloti SM11 (F7X6I3)
brenda