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Information on EC 1.5.5.2 - proline dehydrogenase
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1.5.5.2 proline dehydrogenaseIUBMB 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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Word Map
- 1.5.5.2
-
putas
-
schizophrenia
- pyrroline-5-carboxylate
- delta1-pyrroline-5-carboxylate
-
flavoenzyme
-
psycho
-
hyperprolinemia
-
microdeletion
-
schizoaffective
-
2-acetyl-1-pyrroline
- rgs4
-
velocardiofacial
-
proline-dependent
-
digeorge
-
dysbindin
-
fragrant
- prolidase
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
prodh, proline dehydrogenase, prodh/pox, prodh1, l-proline dehydrogenase, dye-linked l-proline dehydrogenase, puta flavoprotein, ttprodh, jcprodh, tcprodh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.5.99.8
-
-
formerly
-
FAD-dependent L-proline oxidoreductase
L-proline dehydrogenase
L-proline:FAD oxidoreductase
PdhB
PDHbeta
PH1364
PH1751
PRODH
proDH-B1
proDH-B2
PRODH/POX
ProDH1
proline dehydrogenase
bifunctional enzyme: proline utilization A (PutA)
proline dehydrogenase/oxidase
proline oxidase
-
-
-
-
proline/P5C dehydrogenase
bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
PutA
PutA flavoprotein
Tc00.1047053506411.30
TcPRODH
TK0117
TPpdhbeta
TtProDH
L-proline dehydrogenase
-
-
-
-
PutA
bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
PutA flavoprotein
-
combines DNA-binding, proline dehydrogenase and DELTA1-pyrroline-5-carboxylate dehydrogenase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
switching of enzyme from a cytosolic DNA-binding protein to a membrane-bound enzyme involves W211 in a flexible domain near the proline dehydrogenase active site and occurs in a time scale 10fold lower than the turnover number
-
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9050-70-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + ferricyanide + H2O
(S)-1-pyrroline-5-carboxylate + ferrocyanide
-
-
-
?
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
?
-
-
-
?
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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-
-
?
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
a FAD-dependent reaction
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-proline + oxidized phenazine methosulfate
(S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate
-
-
-
-
?
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
L-proline + a quinone
(S)-1-pyrroline-5-carboxylate + a quinol
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
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
FAD
-
FAD may be released by 1 M KBr, apoprotein has no proline dehydrogenase activity but may be restored by external addition of FAD
FAD
determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252
FAD
enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD
FAD
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
FAD
TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559
FMN
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group
additional information
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
-
additional information
-
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
the alpha-subunit contains the [2Fe-2S] iron-sulfur flavoprotein. The gamma subunit is a typical [8Fe-8S] ferredoxin
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-ethylpentyl-barbituric acid
-
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
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
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
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
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
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additional information
no enzyme inhibibtion by atpenin A5, an inhibitor of Complex II
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.