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Information on EC 1.5.99.13 - D-proline dehydrogenase
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1.5.99.13 D-proline dehydrogenaseIUBMB Comments
A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
d-proline dehydrogenase, dye-linked d-proline dehydrogenase, d-pro dh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dye-linked D-proline dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-proline + acceptor = 1-pyrroline-2-carboxylate + reduced acceptor
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
D-proline:acceptor oxidoreductase
A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.
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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
allo-4-hydroxy-D-proline + oxidized 2,6-dichloroindophenol + H2O
? + reduced 2,6-dichloroindophenol
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
D-arginine + oxidized 2,6-dichloroindophenol + H2O
2-oxo-5-guanidinopentanoate + NH3 + reduced 2,6-dichloroindophenol
D-aspartate + oxidized 2,6-dichloroindophenol + H2O
oxaloacetate + NH3 + reduced 2,6-dichloroindophenol
D-glutamate + oxidized 2,6-dichloroindophenol + H2O
2-oxo-glutarate + NH3 + reduced 2,6-dichloroindophenol
23% of the activity with D-proline
-
-
?
D-histidine + oxidized 2,6-dichloroindophenol + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
D-isoleucine + oxidized 2,6-dichloroindophenol + H2O
3-methyl-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
D-leucine + oxidized 2,6-dichloroindophenol + H2O
4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichloroindophenol
D-phenylalanine + oxidized 2,6-dichloroindophenol + H2O
phenylpyruvate + NH3 + reduced 2,6-dichloroindophenol
28% of the activity with D-proline
-
-
?
D-proline + 2,6-dichlorophenolindophenol
1-pyrroline-2-carboxylate + reduced 2,6-dichlorophenolindophenol
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-
-
r
D-proline + oxidized 2,6-dichloroindophenol
DELTA1-pyrroline 2-carboxylate + reduced 2,6-dichloroindophenol
D-proline + oxidized 2,6-dichlorophenolindophenol
DELTA1-pyrroline-2-carboxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-proline + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
DELTA1-pyrroline 2-carboxylate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
33% of the activity with oxidized 2,6-dichloroindophenol
-
-
?
D-proline + oxidized phenazine methosulfate
DELTA1-pyrroline 2-carboxylate + reduced phenazine methosulfate
43% of the activity with oxidized 2,6-dichloroindophenol
-
-
?
D-serine + oxidized 2,6-dichloroindophenol + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
13% of the activity with D-proline
-
-
?
D-threonine + oxidized 2,6-dichloroindophenol + H2O
3-hydroxy-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
15% of the activity with D-proline
-
-
?
D-tryptophan + oxidized 2,6-dichloroindophenol + H2O
3-indole-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
14% of the activity with D-proline
-
-
?
D-valine + oxidized 2,6-dichloroindophenol + H2O
2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol
allo-4-hydroxy-D-proline + oxidized 2,6-dichloroindophenol + H2O
? + reduced 2,6-dichloroindophenol
89% of the activity with D-proline
-
-
?
allo-4-hydroxy-D-proline + oxidized 2,6-dichloroindophenol + H2O
? + reduced 2,6-dichloroindophenol
89% of the activity with D-proline
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
26% of the activity with D-proline
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
-
9% of the activity with D-proline
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
26% of the activity with D-proline
-
-
?
D-arginine + oxidized 2,6-dichloroindophenol + H2O
2-oxo-5-guanidinopentanoate + NH3 + reduced 2,6-dichloroindophenol
10% of the activity with D-proline
-
-
?
D-arginine + oxidized 2,6-dichloroindophenol + H2O
2-oxo-5-guanidinopentanoate + NH3 + reduced 2,6-dichloroindophenol
10% of the activity with D-proline
-
-
?
D-aspartate + oxidized 2,6-dichloroindophenol + H2O
oxaloacetate + NH3 + reduced 2,6-dichloroindophenol
21% of the activity with D-proline
-
-
?
D-aspartate + oxidized 2,6-dichloroindophenol + H2O
oxaloacetate + NH3 + reduced 2,6-dichloroindophenol
-
7% of the activity with D-proline
-
-
?
D-aspartate + oxidized 2,6-dichloroindophenol + H2O
oxaloacetate + NH3 + reduced 2,6-dichloroindophenol
21% of the activity with D-proline
-
-
?
D-histidine + oxidized 2,6-dichloroindophenol + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
-
29% of the activity with D-proline
-
-
?
D-histidine + oxidized 2,6-dichloroindophenol + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
30% of the activity with D-proline
-
-
?
D-isoleucine + oxidized 2,6-dichloroindophenol + H2O
3-methyl-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
-
46% of the activity with D-proline
-
-
?
D-isoleucine + oxidized 2,6-dichloroindophenol + H2O
3-methyl-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
49% of the activity with D-proline
-
-
?
D-leucine + oxidized 2,6-dichloroindophenol + H2O
4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichloroindophenol
-
19% of the activity with D-proline
-
-
?
D-leucine + oxidized 2,6-dichloroindophenol + H2O
4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichloroindophenol
39% of the activity with D-proline
-
-
?
D-proline + oxidized 2,6-dichloroindophenol
DELTA1-pyrroline 2-carboxylate + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-proline + oxidized 2,6-dichloroindophenol
DELTA1-pyrroline 2-carboxylate + reduced 2,6-dichloroindophenol
D-proline is the most preferred substrate among the D-amino acids. 2,6-Dichloroindophenol is the most preferred electron acceptor
-
-
?
D-valine + oxidized 2,6-dichloroindophenol + H2O
2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol
-
18% of the activity with D-proline
-
-
?
D-valine + oxidized 2,6-dichloroindophenol + H2O
2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol
41% of the activity with D-proline
-
-
?
additional information
?
-
ferricyanide, NAD+, NADP+, O2, menadione (vitamin K3), benzyl viologen, horse heart cytochrome c, and methylene blue are inert as electron acceptors
-
-
?
additional information
?
-
-
ferricyanide, NAD+, NADP+, O2, menadione (vitamin K3), benzyl viologen, horse heart cytochrome c, and methylene blue are inert as electron acceptors
-
-
?
additional information
?
-
ferricyanide, NAD+, NADP+, O2, menadione (vitamin K3), benzyl viologen, horse heart cytochrome c, and methylene blue are inert as electron acceptors
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
50% of maximal activity at pH 6.5 and at pH 8.5, proline dehydrogenation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
the activity is linearly increased with increasing temperature to 70°C. The highest activity is above 70°C, and the correct assay is not achieved above 70°C, because of the non-enzymatic decolorization of 2,6-dichloroindophenol
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). DPDH_PYRIL
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)
363
0
40341
Swiss-Prot
-
F9VNI0_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
372
0
41840
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity in the D-Pro dehydrogenase/agar immobilized electrode is retained over 90% for 80 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
energy production
-
a bio-anode using L-glutamate as the fuel is constructed. To oxidize L-glutamate at the anode, glutamate dehydrogenase, derived from Pyrobaculum islandicum, and proline dehydrogenase derived from Pyrococcus horikoshii, are immobilized for a two-enzyme conjugate enzymatic and redox reaction. To achieve an efficient enzyme reaction and electron transfer, the immobilization ratio of proline dehydrogenase to glutamate dehydrogenase is controlled by varying the molar ratios of dithiobis succinimidyl undecanoate and nitrilotriacetic acid dihydrochloride
analysis
-
an amperometric D-amino acid biosensor is prepared with a thermostable D-proline dehydrogenase and a carbon nanotube-ionic liquid gel
analysis
-
development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. The D-Pro DH/agar immobilized electrode is applied to determination of D-amino acids in a human urine sample
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T.
Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase
J. Biol. Chem.
277
12861-12867
2002
Pyrobaculum islandicum (A1RVM8), Pyrobaculum islandicum, Pyrobaculum islandicum JCM 9189 (A1RVM8)
brenda
Tani, Y.; Tanaka, K.; Yabutani, T.; Mishima, Y.; Sakuraba, H.; Ohshima, T.; Motonaka, J.
Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane
Anal. Chim. Acta
619
215-220
2008
Pyrobaculum islandicum
brenda
Tani, Y.; Itoyama, Y.; Nishi, K.; Wada, C.; Shoda, Y.; Satomura, T.; Sakuraba, H.; Ohshima, T.; Hayashi, Y.; Yabutani, T.; Motonaka, J.
An amperometric D-amino acid biosensor prepared with a thermostable D-proline dehydrogenase and a carbon nanotube-ionic liquid gel
Anal. Sci.
25
919-923
2009
Pyrobaculum islandicum
brenda
Sakamoto, H.; Komatsu, T.; Yamasaki, K.; Satomura, T.; Suye, S.
Design of a multi-enzyme reaction on an electrode surface for an L-glutamate biofuel anode
Biotechnol. Lett.
39
235-240
2017
Pyrococcus horikoshii
brenda
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