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Information on EC 1.5.99.B2 - proline dehydrogenase (acceptor)
for references in articles please use BRENDA:EC1.5.99.B2preliminary BRENDA-supplied EC number
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1.5.99.B2 proline dehydrogenase (acceptor)Specify your search results
Word Map
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
Synonyms
dye-linked L-proline dehydrogenase, L-proDH, L-proline dehydrogenase, L-proline: FAD oxidoreductase, L-proline:FAD oxidoreductase, LPDH, PDH, PDH1, PDH2, PF1246, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-proDH
L-proline dehydrogenase
L-proline: FAD oxidoreductase
L-proline:FAD oxidoreductase
LPDH
PDH
PF1798
-
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
PH1364
PH1751
POX
PRODH
ProDH2
proline dehydrogenase
proline oxidase
prub
PutA
TK0117
TK0122
TPpdhB
TPpdhB2
PH1751
-
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
PH1751
-
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
-
proline dehydrogenase
has also a 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) activity
TK0117
-
alpha4beta4-type beta subunit of L-proline dehydrogenase
-
TK0122
-
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
TK0122
-
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
-
TPpdhB
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
TPpdhB
alphabetagammadelta-type beta subunit of L-proline dehydrogenase
-
TPpdhB2
alpha4beta4-type beta subunit of L-proline dehydrogenase
TPpdhB2
alpha4beta4-type beta subunit of L-proline dehydrogenase
-
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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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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-proline:acceptor oxidoreductase
-
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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
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 + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
L-proline + coenzyme Q1 + H2O
DELTA1-pyrroline-5-carboxylate + reduced coenzyme Q1
-
-
-
?
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-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
-
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
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 + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
9% activity compared to 2,6-dichlorophenolindophenol
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
9% activity compared to 2,6-dichlorophenolindophenol
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
?
L-proline + 4-iodonitrotetrazolium violet + H2O
DELTA1-pyrroline-5-carboxylate + reduced 4-iodonitrotetrazolium violet
-
-
-
?
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 + FAD
(S)-1-pyrroline-5-carboxylate + FADH2
-
-
-
?
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-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
-
-
?
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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 + 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
-
-
-
?
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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
-
flavoprotein amine dehydrogenase, the holoenzyme contains one FAD per alphabeta complex
FAD
the beta subunit of the L-proline dehydrogenase complex is the catalytic component containing FAD as a cofactor
FAD
-
ProDH is a flavoenzyme, that can eventually transfer electrons to O2
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no significant effect on activity with 1 mM SrCl2, CaCl2, CoCl2, MgCl2, CuCl2, ZnCl2
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INHIBITOR
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
-
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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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Differential control and function of Arabidopsis ProDH1 and ProDH2 genes upon infection with biotrophic and necrotrophic pathogens.
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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 Tris–HCl, 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 and Haldane kinetics
-
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
-
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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)
0.212
L-proline
with O2 as cosubstrate, in 50 mM Tris-HCl, at 25°C
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
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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
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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
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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
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
located on chromosome22 (22q11.2), region deleted in velo-cardio-facial syndrome
UniProt
brenda
beta-subunit of the L-proline dehydrogenase complex
SwissProt
brenda
beta-subunit of the L-proline dehydrogenase complex
SwissProt
brenda
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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
brenda
additional information
expression levels of ProDH2 are generally low, but increase in senescent leaves and in the abscission zone of floral organs
brenda
expression levels of ProDH2 are generally low, but increase in senescent leaves and in the abscission zone of floral organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
-
proline dehydrogenase (ProDH) is a ubiquitous flavoenzyme involved in the biosynthesis of L-glutamate
-
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
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
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PROD_HUMAN
600
0
68002
Swiss-Prot
Mitochondrion (Reliability: 3)
O50444_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
329
0
36237
TrEMBL
-
O59089_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
382
0
42686
TrEMBL
-
Q6GUH3_TOBAC
499
0
55889
TrEMBL
Mitochondrion (Reliability: 3)
Q6GUH4_TOBAC
499
0
55948
TrEMBL
Mitochondrion (Reliability: 3)
Q6JA03_MEDSA
491
0
54235
TrEMBL
Mitochondrion (Reliability: 3)
PROD2_ARATH
476
0
53074
Swiss-Prot
Mitochondrion (Reliability: 4)
PRODH_THET2
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
307
0
35492
Swiss-Prot
-
Q89E26_BRADU
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
999
0
107366
TrEMBL
-
PRODH_DEIRA
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
310
0
34927
Swiss-Prot
-
Q9YCJ0_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
428
0
46735
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
242000
-
gel filtration, native PAGE leads to two active forms of 24000 and 47000
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
8000
-
isoform PDH2, 1 * 52000, alpha subunit, + 1 * 46000, beta subunit + 1 * 20000, gamma subunit, + 1 * 8000, delta subunit, SDS-PAGE
88000
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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SUBUNIT
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
-
octamer
4 * alpha subunit + 4 * beta subunit, crystallization data
octamer
-
isoform PDH1, 4 * 56000, alpha subunit + 4 * 43000, beta subunit, SDS-PAGE
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
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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PROTEIN VARIANTS
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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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
100
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
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
-
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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meile, L.; Leisinger, T.
Purification and properties of the bifunctional proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase from Pseudomonas aeruginosa
Eur. J. Biochem.
129
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1982
Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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Proline oxidation in corn mitochondia
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567-572
1982
Zea mays
brenda
Mommsen, T.P.; Hochachka, P.W.
Respiratory and enzymatic properties of squid heart mitochondria
Eur. J. Biochem.
120
345-350
1981
Illex illecebrosus
brenda
Balboni, E.; Hecht, R.I.
Studies on the inner mitochondrial membrane localization of proline dehydrogenase
Biochim. Biophys. Acta
462
171-176
1977
Phormia regina
brenda
Kramar, R.
Solubilization of proline dehydrogenase from rat liver mitochondria
Hoppe-Seyler's Z. Physiol. Chem.
352
1267-1270
1971
Rattus norvegicus
brenda
Crabtree, B.; Newsholme, E.A.
The activities of proline dehydrogenase, glutamate dehydrogenase, aspartate-oxoglutarate aminotransferase and alanine-oxoglutarate aminotransferase in some insect flight muscles
Biochem. J.
117
1019-1021
1970
insecta
brenda
Hansford, R.G.; Sacktor, B.
The control of the oxidation of proline by isolated flight muscle mitochondria
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245
991-994
1970
Phormia regina
brenda
Mani, S.; Van de Cotte, B.; Van Montagu, M.; Verbruggen, N.
Altered levels of proline dehydrogenase cause hypersensitivity to proline and its analogs in Arabidopsis
Plant Physiol.
128
73-83
2002
Arabidopsis thaliana
brenda
Tritsch, D.; Mawlawi, H.; Biellmann, J.F.
Mechanism-based inhibition of proline dehydrogenase by proline analogues
Biochim. Biophys. Acta
1202
77-81
1993
Drosophila melanogaster, Glossina morsitans, Rattus norvegicus
brenda
Lee, J.H.; Park, N.Y.; Lee, M.H.; Choi, S.H.
Characterization of the Vibrio vulnificus putAP operon, encoding proline dehydrogenase and proline permease, and its differential expression in response to osmotic stress
J. Bacteriol.
185
3842-3852
2003
Vibrio vulnificus
brenda
Abraham, E.; Rigo, G.; Szekely, G.; Nagy, R.; Koncz, C.; Szabados, L.
Light-dependent induction of proline biosynthesis by abscisic acid and salt stress is inhibited by brassinosteroid in Arabidopsis
Plant Mol. Biol.
51
363-372
2003
Arabidopsis sp.
brenda
Miller, G.; Stein, H.; Honig, A.; Kapulnik, Y.; Zilberstein, A.
Responsive modes of Medicago sativa proline dehydrogenase genes during salt stress and recovery dictate free proline accumulation
Planta
222
70-79
2005
Medicago sativa (Q6JA03)
brenda
White, T.A.; Tanner, J.J.
Cloning, purification and crystallization of Thermus thermophilus proline dehydrogenase
Acta Crystallogr. Sect. F
61
737-739
2005
Thermus thermophilus
brenda
Monaghan, P.J.; Leys D.; Scrutton N.S.
Crystallization and preliminary X-ray diffraction analysis of a flavoenzyme amine dehydrogenase/oxidase from Pyrococcus furiosus DSM 3638
Acta Crystallogr. Sect. F
61
756-758
2005
Pyrococcus furiosus
brenda
Kawakami, R.; Sakuraba, H.; Tsuge, H.; Goda, S.; Katunuma, N.; Ohshima, T.
A second novel dye-linked L-proline dehydrogenase complex is present in the hyperthermophilic archaeon Pyrococcus horikoshii OT-3
FEBS J.
272
4044-4054
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Tsuge, H.; Kawakami, R.; Sakuraba, H.; Ago, H.; Miyano, M.; Aki, K.; Katunuma, N.; Ohshima, T.
Crystal structure of a novel FAD-, FMN-, and ATP-containing L-proline dehydrogenase complex from Pyrococcus horikoshii
J. Biol. Chem.
280
31045-31049
2005
Pyrococcus horikoshii, Pyrococcus horikoshii (O59089), Pyrococcus horikoshii OT-3 (O59089)
brenda
Hu, C.A.; Donald, S.P.; Yu, J.; Lin, W.W.; Liu, Z.; Steel, G.; Obie, C.; Valle, D.; Phang, J.M.
Overexpression of proline oxidase induces proline-dependent and mitochondria-mediated apoptosis
Mol. Cell. Biochem.
295
85-92
2007
Homo sapiens
brenda
Kolodyazhnaya, Y.S.; Titov, S.E.; Kochetov, A.V.; Komarova, M.L.; Romanova, A.V.; Koval, V.S.; Shumny, V.K.
Evaluation of salt tolerance in Nicotiana tabacum plants bearing an antisense suppressor of the proline dehydrogenase gene
Russ. J. Genet.
42
212-214
2006
Nicotiana tabacum
-
brenda
Maxwell, S.A.; Kochevar, G.J.
Identification of a p53-response element in the promoter of the proline oxidase gene
Biochem. Biophys. Res. Commun.
369
308-313
2008
Homo sapiens (O43272)
brenda
White, T.A.; Johnson, W.H.; Whitman, C.P.; Tanner, J.J.
Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine
Biochemistry
47
5573-5580
2008
Thermus thermophilus (Q72IB8)
brenda
Monaghan, P.J.; Leys, D.; Scrutton, N.S.
Mechanistic aspects and redox properties of hyperthermophilic L-proline dehydrogenase from Pyrococcus furiosus related to dimethylglycine dehydrogenase/oxidase
FEBS J.
274
2070-2087
2007
Pyrococcus furiosus
brenda
Huang, T.C.; Huang, Y.W.; Hung, H.J.; Ho, C.T.; Wu, M.L.
DELTA1-pyrroline-5-carboxylic acid formed by proline dehydrogenase from the Bacillus subtilis ssp. natto expressed in Escherichia coli as a precursor for 2-acetyl-1-pyrroline
J. Agric. Food Chem.
55
5097-5102
2007
Bacillus subtilis (Q8RMG1)
brenda
White, T.A.; Krishnan, N.; Becker, D.F.; Tanner, J.J.
Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus
J. Biol. Chem.
282
14316-14327
2007
Thermus thermophilus (Q72IB8)
brenda
Kim, K.Y.; Ahn, J.H.; Cheon, H.G.
Apoptotic action of peroxisome proliferator-activated receptor-gamma activation in human non small-cell lung cancer is mediated via proline oxidase-induced reactive oxygen species formation
Mol. Pharmacol.
72
674-685
2007
Homo sapiens
brenda
Ribarits, A.; Abdullaev, A.; Tashpulatov, A.; Richter, A.; Heberle-Bors, E.; Touraev, A.
Two tobacco proline dehydrogenases are differentially regulated and play a role in early plant development
Planta
225
1313-1324
2007
Nicotiana tabacum (Q6GUH3), Nicotiana tabacum (Q6GUH4)
brenda
Di Rosa, G.; Pustorino, G.; Spano, M.; Campion, D.; Calabro, M.; Aguennouz, M.; Caccamo, D.; Legallic, S.; Sgro, D.L.; Bonsignore, M.; Tortorella, G.
Type I hyperprolinemia and proline dehydrogenase (PRODH) mutations in four Italian children with epilepsy and mental retardation
Psychiatr. Genet.
18
40-42
2008
Homo sapiens
brenda
Kolodyazhnaya, Y.S.; Titov, S.E.; Kochetov, A.V.; Trifonova, E.A.; Romanova, A.V.; Komarova, M.L.; Koval, V.S.; Shumny, V.K.
Tobacco transformants expressing antisense sequence of proline dehydrogenase gene possess tolerance to heavy metals
Russ. J. Genet.
43
825-828
2007
Nicotiana tabacum
-
brenda
Schuermann, J.P.; White, T.A.; Srivastava, D.; Karr, D.B.; Tanner, J.J.
Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicum
Acta Crystallogr. Sect. F
64
949-953
2008
Bradyrhizobium japonicum (Q89E26)
brenda
Phang, J.M.; Donald, S.P.; Pandhare, J.; Liu, Y.
The metabolism of proline, a stress substrate, modulates carcinogenic pathways
Amino Acids
35
681-690
2008
Homo sapiens
brenda
Mitsubuchi, H.; Nakamura, K.; Matsumoto, S.; Endo, F.
Inborn errors of proline metabolism
J. Nutr.
138
2016S-2020S
2008
Homo sapiens (O43272)
brenda
Satomura, T.; Sakuraba, H.; Hara, Y.; Ohshima, T.
Crystallization and preliminary X-ray analysis of a novel dye-linked L-proline dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix
Acta Crystallogr. Sect. F
66
1508-1510
2010
Aeropyrum pernix (Q9YCJ0)
brenda
Funck, D.; Eckard, S.; Mueller, G.
Non-redundant functions of two proline dehydrogenase isoforms in Arabidopsis
BMC Plant Biol.
10
70
2010
Arabidopsis thaliana (Q6NKX1)
brenda
Mohammadi, H.; Omidinia, E.
Proline dehydrogenase from Pseudomonas fluorescens: Gene cloning, purification, characterization and homology modeling
Appl. Biochem. Microbiol.
48
167-174
2012
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
brenda
Satomura, T.; Zhang, X.D.; Hara, Y.; Doi, K.; Sakuraba, H.; Ohshima, T.
Characterization of a novel dye-linked L-proline dehydrogenase from an aerobic hyperthermophilic archaeon, Pyrobaculum calidifontis
Appl. Microbiol. Biotechnol.
89
1075-1082
2011
Pyrobaculum calidifontis, Pyrobaculum calidifontis JCM 11548
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 furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM 12380, Thermococcus profundus (Q76M73), Thermococcus profundus DSM 9503 (Q76M73)
brenda
Luo, M.; Arentson, B.W.; Srivastava, D.; Becker, D.F.; Tanner, J.J.
Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release
Biochemistry
51
10099-10108
2012
Deinococcus radiodurans (Q9RW55)
brenda
Omidinia, E.; Mahdizadehdehosta, R.; Mohammadi, H.
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, Pseudomonas putida POS-F84
brenda
Sakuraba, H.; Satomura, T.; Kawakami, R.; Kim, K.; Hara, Y.; Yoneda, K.; Ohshima, T.
Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix
J. Biol. Chem.
287
20070-20080
2012
Aeropyrum pernix
brenda
Mohammadi, H.S.; Omidinia, E.
Process integration for the recovery and purification of recombinant Pseudomonas fluorescens proline dehydrogenase using aqueous two-phase systems
J. Chromatogr. B
929
11-17
2013
Pseudomonas fluorescens
brenda
Cecchini, N.M.; Monteoliva, M.I.; Alvarez, M.E.
Proline dehydrogenase contributes to pathogen defense in Arabidopsis
Plant Physiol.
155
1947-1959
2011
Arabidopsis thaliana
brenda
Tallarita, E.; Pollegioni, L.; Servi, S.; Molla, G.
Expression in Escherichia coli of the catalytic domain of human proline oxidase
Protein Expr. Purif.
82
345-351
2012
Homo sapiens
brenda
Satomura, T.; Hara, Y.; Suye, S.; Sakuraba, H.; Ohshima, T.
Gene expression and characterization of a third type of dye-linked L-proline dehydrogenase from the aerobic hyperthermophilic archaeon, Aeropyrum pernix
Biosci. Biotechnol. Biochem.
76
589-593
2012
Aeropyrum pernix
brenda
Serrano, H.; Blanchard, J.S.
Kinetic and isotopic characterization of L-proline dehydrogenase from Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
Mycobacterium tuberculosis (O50444), Mycobacterium tuberculosis H37Rv (O50444)
brenda
Monteoliva, M.I.; Rizzi, Y.S.; Cecchini, N.M.; Hajirezaei, M.R.; Alvarez, M.E.
Context of action of proline dehydrogenase (ProDH) in the hypersensitive response of Arabidopsis
BMC Plant Biol.
14
21
2014
Arabidopsis thaliana
brenda
Mohammadi, H.S.; Omidinia, E.
Process integration for the recovery and purification of recombinant Pseudomonas fluorescens proline dehydrogenase using aqueous two-phase systems
J. Chromatogr. B
929
11-17
2013
Pseudomonas fluorescens
brenda
Huijbers, M.; van Berkel, W.
A more polar N-terminal helix releases MBP-tagged Thermus thermophilus proline dehydrogenase from tetramer-polymer self-association
J. Mol. Catal. B
134
340-346
2016
Thermus thermophilus (Q72IB8)
-
brenda
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