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Enzyme Nomenclature
Information on EC 1.5.99.B2 - proline dehydrogenase (acceptor)
for references in articles please use BRENDA:EC1.5.99.B2
Word Map on EC 1.5.99.B2
- 1.5.99.B2
- delta1-pyrroline-5-carboxylate
-
schizophrenia
- pyrroline-5-carboxylate
-
dye-linked
-
necroses
-
de-repressed
-
metabolizable
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autofluorescence
-
syringae
- patatin
- hydroxyproline
- medicine
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.5.99.B2
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
proline dehydrogenase (acceptor)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
also active as 1-pyrroline-5-carboxylate dehydrogenase
-
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
-
-
-
-
L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
-
L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor
ping-pong mechanism, the transfer of hydride from L-proline to FAD is rate-limiting for the reductive half-reaction, but the overall reaction is limited by reduced flavin reoxidation in the second half-reaction. Solvent and multiple kinetic isotope effects suggest that L-proline oxidation occurs in a stepwise rather than concerted mechanism
L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor
ping-pong mechanism, the transfer of hydride from L-proline to FAD is rate-limiting for the reductive half-reaction, but the overall reaction is limited by reduced flavin reoxidation in the second half-reaction. Solvent and multiple kinetic isotope effects suggest that L-proline oxidation occurs in a stepwise rather than concerted mechanism
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-proline:acceptor oxidoreductase
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
located on chromosome22 (22q11.2), region deleted in velo-cardio-facial syndrome
UniProt
beta-subunit of the L-proline dehydrogenase complex
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
proline dehydrogenase (ProDH) is a ubiquitous flavoenzyme involved in the biosynthesis of L-glutamate
metabolism
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proline dehydrogenase (ProDH) is a ubiquitous flavoenzyme involved in the biosynthesis of L-glutamate
-
physiological function
the monofunctional proline dehydrogenase (ProDH) performs the flavin-dependent oxidation of L-proline to DELTA1-pyrroline-5-carboxylate in the proline catabolic pathway
physiological function
-
proline (Pro) dehydrogenase (ProDH) catalyzes the rate limiting step in the oxidation pathway, transferring two electrons from Pro to the noncovalently bound FAD cofactor to subsequently deliver these electrons to a final acceptor. The plant enzyme sustains oxidative phosphorylation and ATP generation using endogenous electron acceptors. ProDH potentiates the oxidative burst and cell death of the plant hypersensitive response. ProDH converts Pro into DELTA1 pyrroline-5-carboxylate (P5C) and can act together with P5C dehydrogenase (P5CDH) to produce Glu, or with P5C reductase (P5CR) to regenerate Pro and thus stimulate the Pro/P5C cycle. ProDH activation has different effects on hypersensitive response. Before the oxidative burst it leads to Pro consumption involving the action of P5CDH. During the oxidative burst, ProDH becomes functionally uncoupled to P5CDH and apparently works with P5C reductase. The absence of P5CDH does not reduce reactive oxygen species, cell death, or pathogen resistance, indicating this enzyme is not accompanying ProDH in the potentiation of these defense responses. In contrast, p5cdh infected mutant plants display increased reactive oxygen species burst and earlier initiation of hypersensitive response cell death. ProDH may sustain hypersensitive response by participating in the Pro/P5C cycle. Evaluation of ProDH action at different hypersensitive response stages, overview
physiological function
-
the monofunctional proline dehydrogenase (ProDH) performs the flavin-dependent oxidation of L-proline to DELTA1-pyrroline-5-carboxylate in the proline catabolic pathway
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additional information
residue Y203 serves to bind and orient L-proline in the active site, residue K110 is the active site base observed in the pH profile
additional information
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residue Y203 serves to bind and orient L-proline in the active site, residue K110 is the active site base observed in the pH profile
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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
3,4-dehydro-L-proline + acceptor + H2O
? + reduced acceptor
-
efficient substrate
-
-
?
4-methylene-L-proline + acceptor + H2O
DELTA1-pyrroline-3-methylene-5-carboxylic acid + reduced acceptor
-
-
-
?
L-hydroxyproline + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
L-hydroxyproline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
100% activity compared to L-proline
-
-
?
L-hydroxyproline + oxidized 2,6-dichlorophenolindophenol + H2O
?
-
reaction rate is 39% of that with L-proline
-
-
?
L-leucine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
42% activity compared to L-proline
-
-
?
L-proline + 2,6-dichlorophenolindophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
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-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium
L-proline + coenzyme Q1 + H2O
DELTA1-pyrroline-5-carboxylate + reduced coenzyme Q1
-
-
-
?
L-proline + FAD
(S)-1-pyrroline-5-carboxylate + FADH2
Q89E26
-
-
-
?
L-proline + oxidized 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
the enzyme does not utilize ferricyanide or 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl-tetrazolium bromide as the electron acceptor, activity with phenazine methosulfate-p-iodonitrotetrazolium violet is 10% of that with 2,6-dichlorophenolindophenol
-
-
?
L-proline + oxidized phenazine methosulfate
(S)-1-pyrroline-5-carboxylate + reduced phenazine methosulfate
-
-
-
-
?
L-proline + p-iodonitrotetrazolium + H2O
(S)-1-pyrroline-5-carboxylate + reduced p-iodonitrotetrazolium
-
-
-
?
L-proline + phenazine methosulfate 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium
-
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
L-serine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
55% activity compared to L-proline
-
-
?
L-threonine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
66% activity compared to L-proline
-
-
?
L-valine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
33% activity compared to L-proline
-
-
?
glycine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
52% activity compared to L-proline
-
-
?
glycine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
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52% activity compared to L-proline
-
-
?
L-alanine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
48% activity compared to L-proline
-
-
?
L-alanine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
48% activity compared to L-proline
-
-
?
L-alanine + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
?
-
weak activity
-
-
?
L-alanine + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
?
-
weak activity
-
-
?
L-arginine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
62% activity compared to L-proline
-
-
?
L-arginine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
62% activity compared to L-proline
-
-
?
L-histidine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
72% activity compared to L-proline
-
-
?
L-histidine + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
72% activity compared to L-proline
-
-
?
L-hydroxyproline + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
72% activity compared to L-proline
-
-
?
L-hydroxyproline + 2,6-dichlorophenolindophenol + H2O
? + reduced 2,6-dichlorophenolindophenol
-
72% activity compared to L-proline
-
-
?
L-proline + 2,6-dichlorophenolindophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
artificial electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
L-proline is the most preferred substrate and 2,6-dichlorophenolindophenol is the most preferred electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
L-proline is the most preferred substrate and 2,6-dichlorophenolindophenol is the most preferred electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
-
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2,6-dichlorophenolindophenol + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol
the alphabetagammadelta-type beta subunit of L-proline dehydrogenase prefers 2, 6-dichloroindophenol as electron acceptor
-
-
?
L-proline + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium
-
-
-
-
?
L-proline + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium
-
-
-
-
?
L-proline + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
DELTA1-pyrroline-5-carboxylate + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium
-
-
-
-
?
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
-
?
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
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
-
-
-
ir
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
highly specific for L-form of proline
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
preferred substrate
-
-
?
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
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
?
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
-
-
-
?
L-proline + acceptor + H2O
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, menadione, cytochrome c
-
?
L-proline + cytochrome c + H2O
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
-
?
L-proline + cytochrome c + H2O
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
93% activity compared to 2,6-dichlorophenolindophenol
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
93% activity compared to 2,6-dichlorophenolindophenol
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + ferricyanide
DELTA1-pyrroline-5-carboxylate + ferrocyanide
the alpha4beta4-type beta subunit of L-proline dehydrogenase utilizes ferricyanide as the most preferable electron acceptor
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
9% activity compared to 2,6-dichlorophenolindophenol
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
9% activity compared to 2,6-dichlorophenolindophenol
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
?
L-proline + phenazine methosulfate-4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced phenazine methosulfate-4-iodonitrotetrazolium violet
-
-
-
?
L-threonine + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
?
-
weak activity
-
-
?
L-threonine + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O
?
-
weak activity
-
-
?
additional information
?
-
-
no activity with: D-proline, glycine, L-glutamate, L-aspartate, L-arginine, L-lysine, L-serine, L-leucine, L-alanine, L-threonine, L-methionine,L-tryptophan, L-tyrosine
-
-
-
additional information
?
-
-
no activity with D-proline, L-tryptophan, L-glutamate, and L-aspartate
-
-
-
additional information
?
-
-
no activity with D-proline, L-tryptophan, L-glutamate, and L-aspartate
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, L-arginine, L-aspartate, and glycine are inert as substrates
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, L-arginine, L-aspartate, and glycine are inert as substrates
-
-
-
additional information
?
-
-
sarcosine, D-proline, L-ornithine, L-glutamate, L-arginine, L-serine, L-leucine, L-valine, and L-alanine are inert as substrates. NAD+, NADP+, and bovine heart cytochrome c are inert as electron acceptors
-
-
-
additional information
?
-
-
sarcosine, D-proline, L-ornithine, L-glutamate, L-arginine, L-serine, L-leucine, L-valine, and L-alanine are inert as substrates. NAD+, NADP+, and bovine heart cytochrome c are inert as electron acceptors
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
-
isoform PDH1, no substrate: L-hydroxyproline, D-proline, cis-4-hydroxy-D-proline, L-2-pyrrolidone-5-carboxylate, pyrrole-5-carboxylate, pipecolic acid
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
-
isoform PDH1, no substrate: L-hydroxyproline, D-proline, cis-4-hydroxy-D-proline, L-2-pyrrolidone-5-carboxylate, pyrrole-5-carboxylate, pipecolic acid
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
D-proline, L-hydroxyproline, pyrrolidone-5-carboxylate, sarcosine, and glycine are inert as substrates
-
-
-
additional information
?
-
-
trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline, L-azetidine-2-carboxylic acid, and L-pipecolinic acid are no substrates of PRODH
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
-
-
-
-
?
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
O50444
-
-
-
?
L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
O50444
-
-
-
?
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
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
isoform PDH1, 1 mol per mol of beta subunit, alpha and beta subunits separatively produced in Escherichia coli cannot bind FAD
FAD
; the beta subunit of the L-proline dehydrogenase complex is the catalytic component containing FAD as a cofactor
FAD
-
flavoprotein amine dehydrogenase, the holoenzyme contains one FAD per alphabeta complex
FAD
-
ProDH is a flavoenzyme, that can eventually transfer electrons to O2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no significant effect on activity with 1 mM SrCl2, CaCl2, CoCl2, MgCl2, CuCl2, ZnCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
inhibited by salt-stress in shoots and roots of light-grown plants
-
additional information
-
trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline, L-azetidine-2-carboxylic acid, and L-pipecolinic acid are no inhibitors of PRODH
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-proline
-
in the presence of L-proline, high POX activity is sufficient to induce mitochondria-mediated apoptosis
additional information
-
POX mRNA expression, and the extent of POX induction is correlated with radical oxygen species level and cell death suggesting that POX-induced radical oxygen species formation is critical for the apoptotic cell death induced by PPARgamma activation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
212.3
L-Pipecolic acid
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
0.026
2,6-dichlorophenolindophenol
-
with L-proline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
0.035
2,6-dichlorophenolindophenol
-
with L-hydroxyproline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C
3.4
2,6-dichlorophenolindophenol
pH 7.1, 25°C, recombinant wild-type enzyme
0.028
coenzyme Q1
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.032
coenzyme Q1
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.155
coenzyme Q1
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.174
L-proline
-
PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
0.334
L-proline
-
PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
0.689
L-proline
-
PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
1.46
L-proline
-
TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
1.95
L-proline
-
mutant enzyme Y215F, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
2.38
L-proline
-
TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
2.46
L-proline
TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
2.5 - 5
L-proline
-
PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
3.5
L-proline
TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
5.3
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 50°C
5.6
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 40°C
6.5
L-proline
-
pH 7.4, 45°C, recombinant wild-type enzyme, Haldane kinetics
9.9
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
11.5
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Michaelis-Menten kinetics
14.46
L-proline
-
mutant enzyme H225Q, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
16.5
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Haldane kinetics
19.67
L-proline
-
mutant enzyme H225A, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
19.9
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 70°C
27
L-proline
-
with 2,6-dichlorophenolindophenol as cosubstrate, in 50 mM Tris-HCl, at 25°C
30.8
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
31
L-proline
-
in 100 mM TrisHCl, 10 mM MgCl2, 10% (v/v) glycerol, pH 8.5, at 25°C
33.8
L-proline
-
pH 7.4, 45°C, recombinant mutant F10E/L12E, Haldane kinetics
50
L-proline
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
67.6
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Michaelis-Menten kinetics
175.1
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Haldane kinetics
290
L-proline
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
384
L-proline
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
additional information
additional information
Michaelis-Menten kinetics, steady-state kinetics and pre-steady-state kinetics of wild-type and mutant enzymes, stopped-flow kinetic isotope effects, bisubstrate kinetic analysis, overview
-
additional information
additional information
-
Michaelis-Menten and Haldane kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
L-Pipecolic acid
-
wild type enzyme in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
0.043
coenzyme Q1
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.046
coenzyme Q1
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
14
coenzyme Q1
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.055
L-proline
mutant enzyme E64A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.08
L-proline
mutant enzyme G63A, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
0.4
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 40°C
1.3
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 50°C
1.4
L-proline
-
mutant enzyme H225A, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
1.96
L-proline
-
PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
3.49
L-proline
-
PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
3.7
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Michaelis-Menten kinetics
3.91
L-proline
-
PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
4
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
4.4
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Haldane kinetics
6.22
L-proline
TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
8.7
L-proline
wild type enzyme, at 23°C, in 50 mM potassium phosphate and 25 mM NaCl (pH 7.5)
8.97
L-proline
-
mutant enzyme H225Q, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
9.8
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Michaelis-Menten kinetics
10.4
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 70°C
11
L-proline
-
PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
11.6
L-proline
-
TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
13
L-proline
-
with 2,6-dichlorophenolindophenol as cosubstrate, in 50 mM Tris-HCl, at 25°C
18.01
L-proline
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.5, at 80°C
19.4
L-proline
-
pH 7.4, 45°C, recombinant wild-type enzyme, Haldane kinetics
20
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Haldane kinetics
27.6
L-proline
-
TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
27.9
L-proline
TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
37.17
L-proline
-
mutant enzyme Y215F, in 100 mM potassium phosphate buffer, pH 7.5, at 60°C
42.1
L-proline
-
pH 7.4, 45°C, recombinant mutant F10E/L12E, Haldane kinetics
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.114
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Haldane kinetics
0.146
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Michaelis-Menten kinetics
0.269
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Haldane kinetics
0.325
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Michaelis-Menten kinetics
1.247
L-proline
-
pH 7.4, 45°C, recombinant mutant F10E/L12E, Haldane kinetics
2.979
L-proline
-
pH 7.4, 45°C, recombinant wild-type enzyme, Haldane kinetics
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
171
L-proline
-
pH 7.4, 45°C, recombinant mutant F10E/L12E, Haldane kinetics
206
L-proline
-
pH 7.4, 25°C, recombinant mutant F10E/L12E, Haldane kinetics
306
L-proline
-
pH 7.4, 45°C, recombinant wild-type enzyme, Haldane kinetics
825
L-proline
-
pH 7.4, 25°C, recombinant wild-type enzyme, Haldane kinetics
24
L-pyroglutamate
-
PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
49.4
L-pyroglutamate
-
TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
55.5
L-pyroglutamate
-
PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
56.1
L-pyroglutamate
TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
68.3
L-pyroglutamate
-
PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
122
L-pyroglutamate
TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
129
L-pyroglutamate
-
PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
167
L-pyroglutamate
-
TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
600
-
purified recombinant enzyme in an optimized aqueous two-phase system containing 14% w/w PEG-1000 and 12% w/w Na2CO3, pH 8.0, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
45
-
assay at, both for recombinant MBP-tagged wild-type and mutant enzyme, kcat increases when the temperature is raised from 25°C to 45°C, the temperature is not increased further due to the instability of the MBP-tag
65
80
65
-
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
65
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
more than 60% activity between 20-40°C, a sharp decrease is observed above 30°C and enzyme activity is completely inactivated at 70°C
25 - 45
-
remarkable 10fold increase in catalytic efficiency from 25°C to 45°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression levels of ProDH2 are generally low, but increase in senescent leaves and in the abscission zone of floral organs
strongest expression in microspore; strongest expression in microspore
strong expression in mature pollen; strong expression in mature pollen
additional information
expression levels of ProDH2 are generally low, but increase in senescent leaves and in the abscission zone of floral organs
expression levels of ProDH2 are generally low, but increase in senescent leaves and in the abscission zone of floral organs
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8000
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
20000
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
40000
43000
-
isoform PDH1, 4 * 56000, alpha subunit + 4 * 43000, beta subunit, SDS-PAGE
46000
52000
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
55000
56000
-
isoform PDH1, 4 * 56000, alpha subunit + 4 * 43000, beta subunit, SDS-PAGE
88000
242000
-
gel filtration, native PAGE leads to two active forms of 24000 and 47000
46000
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotetramer
homodimer
monomer
octamer
additional information
-
MBP-TtProDH and MBP-clipped TtProDH are prone to aggregation through non-native self-association. The hydrophobic N-terminal helix of TtProDH is responsible for the self-association process
heterotetramer
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
heterotetramer
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
-
homodimer
-
2 * 46000, SDS-PAGE; 2 * 46259, calculated from amino acid sequence
homodimer
-
2 * 46000, SDS-PAGE; 2 * 46259, calculated from amino acid sequence
-
octamer
-
isoform PDH1, 4 * 56000, alpha subunit + 4 * 43000, beta subunit, SDS-PAGE
octamer
4 * alpha subunit + 4 * beta subunit, crystallization data
octamer
-
isoform PDH1, 4 * 56000, alpha subunit + 4 * 43000, beta subunit, SDS-PAGE
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme bound with L-proline, sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M trisodium citrate dihydrate (pH 5.6), and 30% (w/v) polyethylene glycol 4000
-
His-tag removed, three crystal forms: apparent tetragonal, hexagonal and centered monoclinic
Q89E26
enzyme in the oxidized state complexed with the proline analogue L-tetrahydrofuroic acid and in the reduced state with the proline site vacant, sitting drop vapor diffusion method, using 0.2 M MgCl2, 25% (w/v) PEG 3350, and 0.1 mM Bis-Tris (pH 5.8), at 22°C
beta subunit is the L-proline dehydrogenase catalytic component and contains FAD, alpha subunit has a classical dinucleotide fold domain with ATP and a Cys-clustered domain. FMN is located at the interface of alpha and beta subunits; crystal structure of PDH1, which is a heterooctameric complex containing three different cofactors: FAD, FMN, and ATP. The structure is determined by x-ray crystallography to a resolution of 2.86 A. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, is similar to that of monomeric sarcosine oxidase
analysis of the three-dimensional model of TtProDH crystal structure, PDB ID 2G37
-
from a monodisperse protein solution with detergent n-octyl beta-D-glucopyranoside
-
sitting drop vapour diffusion method, with 100 mM imidazole (pH 7), 100 mM MgCl2, 17% 2-methyl-2,4-pentanediol, and 5 mM dithiothreitol
-
sitting drop vapour diffusion method, with 100 mM imidazole buffer at pH 7, 100 mM MgCl2, 14% 2-methyl-2,4-pentanediol, and 5 mM dithiothreitol
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9
-
the enzyme retains more than 90% of its activity after incubation at pH values 4.5-9.0 for 30 min at 50°C
724048
5 - 10
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
the enzyme loses a considerable amount of its original activity at above 30°C and is nearly inactivated at 70°C
45
the enzyme loses 70% of activity upon incubation at 45°C for 15 min
70
90
100 - 105
-
the enzyme retains more than 90% of its activity after incubation at 100°C for 120 min (pH 7.5). The half-life at 105°C is about 90 min
100
-
no loss of activity being evident up to 100°C, above this temperature, thermal denaturation of PRODH is apparent, with complete loss of activity after 10 min of incubation in glycerol buffer at temperatures above 115°C
70
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase retains more than 80% of activity after heating at 70°C for 20 min, while the alphabetagammadelta-type beta subunit of L-proline dehydrogenase retains 100% activity under the same conditions
70
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase retains more than 80% of activity after heating at 70°C for 20 min, while the alphabetagammadelta-type beta subunit of L-proline dehydrogenase nearly loses all of its activity under the same conditions
70
-
the alpha4beta4-type beta subunit of L-proline dehydrogenase retains more than 80% of activity after heating at 70°C for 20 min, while the alphabetagammadelta-type beta subunit of L-proline dehydrogenase shows 76% activity under the same conditions
70
the alpha4beta4-type beta subunit of L-proline dehydrogenase retains more than 80% of activity after heating at 70°C for 20 min, while the alphabetagammadelta-type beta subunit of L-proline dehydrogenase shows 68% activity under the same conditions
90
-
PRODH exhibits over 85% residual activity after a 1 h incubation at 90°C and over 60% residual activity after 3 h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Toyopearl 650M column chromatography and Superdex 200 gel filtration
-
HisTrap column chromatography and Hitrap Q column chromatography
Ni-chelating column chromatography
Ni2+-charged chelating Sepharose column chromatography and Sephacryl S-300 gel filtration
-
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Mycobacterium smegmatis mc24517 cells by nickel affinity chromatography
recombinant enzyme
recombinant enzyme via refolding, reconstitution and two-phase partitioning in an optimized aqueous two-phase system, containing 14% w/w PEG-1000 and 12% w/w Na2CO3 at pH 8.0, from Escherichia coli strain BL21 (DE3) plysS inclusion bodies in one step, method optimization and evaluation, overview
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL and BL21-Gold(DE3)pLysS cells
recombinant expression of the enzyme in Escherichia coli strain BL21 (DE3) plysS inclusion bodies
-
recombinant overexpression of C-terminally His6-tagged wild-type and mutant enzymes in Mycobacterium smegmatis mc24517 cells using vector pYUB1062
recombinant overexpression of wild-type and mutant MBP-fusion enzyme in Escherichia coli TOP 10 cells, MBP-TtProDH and MBP-clipped TtProDH are proneto aggregation through non-native self-association
-
the two MsPDH genes MsPDH1 and MsPDH2 share a high nucleotide sequence homology and a similar exon/intron structure
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL and BL21-Gold(DE3)pLysS cells
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL and BL21-Gold(DE3)pLysS cells
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL and BL21-Gold(DE3)pLysS cells
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL and BL21-Gold(DE3)pLysS cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
oxidative burst causes a hypersensitive response with induction of proline dehydrogenase (ProDH), the plants do not consume Pro during maximal reactive oxygen species accumulation, and maintain almost basal DELTA1 pyrroline-5-carboxylate levels at all conditions. Mutant plants lacking DELTA1 pyrroline-5-carboxylate dehydrogenase activate ProDH like the wild-type plants. Under cold acclimation, ProDH induction is accompanied by Pro increase. ProDH activation occuring after stress release does not always be accompanied by P5CDH and can have minor effects on the Pro content
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y203F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y203F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H225A
-
the mutant is unstable and precipitates from solution below pH 7.0, decreased activity compared to the wild type enzyme
H225Q
-
the mutant displays activity down to solution pH 6.0, increased activity compared to the wild type enzyme
Y251F
-
wild type pH stability, increased activity compared to the wild type enzyme
F10E/L12E
-
two point mutations in helix alphaA. This helix contains several hydrophobic residues. The recombinant MBP-tagged mutant variant exclusively forms tetramers and exhibits excellent catalytic features over a wide range of temperatures
additional information
additional information
-
plants with altered levels of enzyme by sense and antisense strategies
additional information
-
mutant plants lacking DELTA1 pyrroline-5-carboxylate dehydrogenase activate ProDH during hypersensitive response like the wild-type plants. They achieve maximum oxidative burst and cell death levels producing normal hypersensitive response lesions, but evidence premature defense activation
additional information
-
transgenic plants bearing an antisense suppressor of enzyme have elevated salt tolerance and increased resistance to toxic proline analogue L-azetidine-2-carboxylic acid
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme via refolding, reconstitution and two-phase partitioning in an optimized aqueous two-phase system, containing 14% w/w PEG-1000 and 12% w/w Na2CO3 at pH 8.0, from Escherichia coli strain BL21 (DE3) plysS inclusion bodies in one step
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.99.B2)
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