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Information on EC 1.4.99.6 - D-arginine dehydrogenase
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1.4.99.6 D-arginine dehydrogenaseIUBMB Comments
Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25, L-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
d-amino acid dehydrogenase, d-alanine dehydrogenase, d-arginine dehydrogenase, daadh, d-amino acid dehydrogenase dada, nadp+-dependent d-amino acid dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-amino acid dehydrogenase
DAADH
DAD
DadA
DADH
DauA
EC 1.4.99.1
-
-
formerly
-
NADP+-dependent D-amino acid dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arginine + acceptor = iminoarginine + reduced acceptor
(1a)
-
-
-
iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3
(1b), spontaneous
-
-
-
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor
a flavoprotein, FAD
-
-
-
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor
A flavoprotein, FAD. Acts to some extent on all D-amino acids, except D-aspartate and D-glutamate
-
-
-
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
D-arginine:acceptor oxidoreductase (deaminating)
Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25, L-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine.
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CAS REGISTRY NUMBER
COMMENTARY
37205-44-0
-
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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
D-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
D-alanine + H2O + 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
D-alanine + H2O + methylene blue
pyruvate + NH3 + reduced methylene blue
-
low activity
-
?
D-arginine + H2O + FAD
5-guanidino-2-oxopentanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-arginine + H2O + iodonitrotetrazolium chloride
5-guanidino-2-oxopentanoate + NH3 + reduced iodonitrotetrazolium chloride
-
D-arginine and D-lysine are the most effective substrates
-
-
?
D-arginine + phenazine methosulfate
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
D-arginine + phenazine methosulfate + H2O
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
D-Asp + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxobutanedioate + NH3 + reduced 2,6-dichlorophenolindophenol
D-asparagine + H2O + 2,6-dichlorophenolindophenol
2-oxosuccinamic acid + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-asparagine + H2O + methylene blue
2-oxosuccinamic acid + NH3 + reduced methylene blue
-
-
-
?
D-asparagine + phenazine methosulfate + H2O
2-oxobutanedioate + NH3 + reduced phenazine methosulfate
D-cysteine + H2O + methylene blue
3-mercapto-2-oxopropanoate + NH3 + reduced methylene blue
-
-
-
?
D-cystine + H2O + methylene blue
? + NH3 + reduced methylene blue
-
-
-
?
D-Glu + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxoglutarate + NH3 + reduced 2,6-dichlorophenolindophenol
D-glutamine + phenazine methosulfate + H2O
5-amino-2,5-dioxopentanoate + NH3 + reduced phenazine methosulfate
D-histidine + H2O + 2,6-dichlorophenolindophenol
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-histidine + H2O + FAD
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-histidine + H2O + iodonitrotetrazolium chloride
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
D-histidine + H2O + methylene blue
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced methylene blue
-
-
-
?
D-histidine + phenazine methosulfate
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
D-histidine + phenazine methosulfate + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-isoleucine + H2O + 2,6-dichlorophenolindophenol
3-methyl-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-isoleucine + H2O + methylene blue
3-methyl-2-oxopentanoate + NH3 + reduced methylene blue
-
-
-
?
D-isoleucine + phenazine methosulfate + H2O
3-methyl-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-kynurenine + H2O + 2,6-dichlorophenolindophenol
4-(2-aminophenyl)-2,4-dioxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-kynurenine + H2O + methylene blue
4-(2-aminophenyl)-2,4-dioxobutanoate + NH3 + reduced methylene blue
-
-
-
?
D-leucine + H2O + 2,6-dichlorophenolindophenol
4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-leucine + H2O + methylene blue
4-methyl-2-oxopentanoate + NH3 + reduced methylene blue
-
-
-
?
D-leucine + phenazine methosulfate + H2O
4-methyl-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-lysine + H2O + iodonitrotetrazolium chloride
7-amino-2-oxoheptanoic acid + NH3 + reduced iodonitrotetrazolium chloride
-
D-arginine and D-lysine are the most effective substrates
-
-
?
D-lysine + phenazine methosulfate
6-amino-2-oxohexanoate + NH3 + reduced phenazine methosulfate
D-lysine + phenazine methosulfate + H2O
7-amino-2-oxoheptanoic acid + NH3 + reduced phenazine methosulfate
-
-
-
?
D-Met + H2O + oxidized 2,6-dichlorophenolindophenol
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
D-methionine + H2O + 2,6-dichlorophenolindophenol
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-methionine + H2O + iodonitrotetrazolium chloride
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
D-methionine + phenazine methosulfate
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced phenazine methosulfate
D-methionine + phenazine methosulfate + H2O
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-norleucine + H2O + 2,6-dichlorophenolindophenol
2-oxohexanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-norleucine + H2O + methylene blue
2-oxohexanoate + NH3 + reduced methylene blue
-
-
-
?
D-norvaline + H2O + methylene blue
2-oxopentanoate + NH3 + reduced methylene blue
-
-
-
?
D-ornithine + H2O + iodonitrotetrazolium chloride
? + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
D-Phe + H2O + oxidized 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
19.8% activity compared to D-Pro
-
-
?
D-phenylalanine + H2O + 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
D-phenylalanine + H2O + FAD
phenylpyruvate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-phenylalanine + H2O + iodonitrotetrazolium chloride
phenylpyruvate + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
D-phenylalanine + H2O + methylene blue
phenylpyruvate + NH3 + reduced methylene blue
-
-
-
?
D-phenylalanine + phenazine methosulfate
2-oxo-3-phenylpropanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-phenylalanine + phenazine methosulfate + H2O
2-oxo-3-phenylpropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-Pro + H2O + oxidized 2,6-dichlorophenolindophenol
DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol
100% activity
-
-
?
D-proline + H2O + 2,6-dichlorophenolindophenol
DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-proline + H2O + coenzyme Q1
DELTA1-pyrroline-2-carboxylate + NH3 + reduced coenzyme Q1
-
-
-
?
D-proline + H2O + FAD
2-oxopentanoic acid + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-proline + phenazine methosulfate + H2O
DELTA1-pyrroline-2-carboxylate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-Ser + H2O + oxidized 2,6-dichlorophenolindophenol
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
6.7% activity compared to D-Pro
-
-
?
D-serine + H2O + 2,6-dichlorophenolindophenol
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
D-serine + H2O + FAD
3-hydroxy-2-oxopropanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-serine + H2O + methylene blue
3-hydroxy-2-oxopropanoate + NH3 + reduced methylene blue
-
low activity
-
?
D-serine + phenazine methosulfate + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-threonine + H2O + 2,6-dichlorophenolindophenol
3-hydroxy-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
low activity
-
?
D-threonine + H2O + FAD
3-hydroxy-2-oxobutanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-threonine + H2O + methylene blue
3-hydroxy-2-oxobutanoate + NH3 + reduced methylene blue
-
low activity
-
?
D-threonine + phenazine methosulfate + H2O
3-hydroxy-2-oxobutanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-tryptophan + H2O + 2,6-dichlorophenolindophenol
3-indole-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-tryptophan + H2O + methylene blue
3-indole-2-oxopropanoate + NH3 + reduced methylene blue
-
-
-
?
D-tryptophan + phenazine methosulfate + H2O
3-indole-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-tyrosine + H2O + 2,6-dichlorophenolindophenol
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-tyrosine + H2O + FAD
(4-hydroxyphenyl)pyruvate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-tyrosine + H2O + iodonitrotetrazolium chloride
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
D-tyrosine + H2O + methylene blue
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced methylene blue
-
-
-
?
D-tyrosine + phenazine methosulfate
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-tyrosine + phenazine methosulfate + H2O
(4-hydroxyphenyl)pyruvate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-Val + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
0.8% activity compared to D-Pro
-
-
?
D-valine + H2O + 2,6-dichlorophenolindophenol
2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-valine + H2O + FAD
2-oxopentanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-valine + H2O + methylene blue
2-oxoisopentanoate + NH3 + reduced methylene blue
-
-
-
?
D-valine + phenazine methosulfate + H2O
2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
L-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
?
1.9% activity compared to D-Pro
-
-
?
L-Pro + H2O + oxidized 2,6-dichlorophenolindophenol
?
3.5% activity compared to D-Pro
-
-
?
(3S,3R)-2-oxo-3-methylvaleric acid + NH3 + NADPH + H+
D-isoleucine + H2O + NADP+
-
-
yield of 45% after incubation for 1 h at 50 °C
-
?
(3S,3R)-2-oxo-3-methylvaleric acid + NH3 + NADPH + H+
D-isoleucine + H2O + NADP+
-
-
yield of 45% after incubation for 1 h at 50 °C
-
?
2-oxo-3-methylbutyric acid + NH3 + NADPH + H+
D-valine + H2O + NADP+
-
-
yield of 83% after incubation for 1 h at 50 °C
-
?
2-oxo-3-methylbutyric acid + NH3 + NADPH + H+
D-valine + H2O + NADP+
-
-
yield of 83% after incubation for 1 h at 50 °C
-
?
2-oxo-4-methylvaleric acid + NH3 + NADPH + H+
D-leucine + H2O + NADP+
-
-
yield of 91% after incubation for 1 h at 50 °C
-
?
2-oxo-4-methylvaleric acid + NH3 + NADPH + H+
D-leucine + H2O + NADP+
-
-
yield of 91% after incubation for 1 h at 50 °C
-
?
D-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
36.8% activity compared to D-Pro
-
-
?
D-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
36.8% activity compared to D-Pro
-
-
?
D-alanine + H2O + 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-alanine + H2O + 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
low activity
-
?
D-alanine + H2O + FAD
pyruvate + NH3 + FADH2
D-amino acid dehydrogenase activity of broad substrate specificity
-
-
?
D-alanine + H2O + FAD
pyruvate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-alanine + phenazine methosulfate + H2O
pyruvate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-alanine + phenazine methosulfate + H2O
pyruvate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-arginine + phenazine methosulfate
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-arginine + phenazine methosulfate
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
overall reaction
-
?
D-arginine + phenazine methosulfate
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-arginine + phenazine methosulfate
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
fast substrate D-arginine leads to a dead-end complex of the reduced enzyme and the substrate at high concentrations of D-arginine yielding substrate inhibition, while the overall turnover is partially limited by the release of the iminoarginine product
overall reaction
-
?
D-arginine + phenazine methosulfate + H2O
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-arginine + phenazine methosulfate + H2O
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-arginine + phenazine methosulfate + H2O
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-arginine + phenazine methosulfate + H2O
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-Asp + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxobutanedioate + NH3 + reduced 2,6-dichlorophenolindophenol
0.8% activity compared to D-Pro
-
-
?
D-Asp + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxobutanedioate + NH3 + reduced 2,6-dichlorophenolindophenol
0.8% activity compared to D-Pro
-
-
?
D-asparagine + phenazine methosulfate + H2O
2-oxobutanedioate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-asparagine + phenazine methosulfate + H2O
2-oxobutanedioate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-Glu + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxoglutarate + NH3 + reduced 2,6-dichlorophenolindophenol
1.0% activity compared to D-Pro
-
-
?
D-Glu + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxoglutarate + NH3 + reduced 2,6-dichlorophenolindophenol
1.0% activity compared to D-Pro
-
-
?
D-glutamine + phenazine methosulfate + H2O
5-amino-2,5-dioxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-glutamine + phenazine methosulfate + H2O
5-amino-2,5-dioxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-histidine + phenazine methosulfate
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-histidine + phenazine methosulfate
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
slow substrate, the initial Michaelis complex undergoes an isomerization involving multiple conformations that are not all equally catalytically competent for the subsequent oxidation reaction, while the overall turnover is at least partially limited by flavin reduction
-
-
?
D-leucine + phenazine methosulfate
? + NH3 + reduced phenazine methosulfate
-
-
-
?
D-leucine + phenazine methosulfate
? + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-leucine + phenazine methosulfate
? + NH3 + reduced phenazine methosulfate
enzyme preferentially binds the zwitterionic form of the substrate. Isomerization of the Michaelis complex yields an enzyme-substrate complex competent for flavin reduction. Amine deprotonation triggers the oxidation reaction, with cleavage of the substrate NH and CH bonds occurring in an asynchronous fashion. Tyr53, on a mobile loop covering the active site, may participate in substrate binding and facilitate flavin reduction
-
-
?
D-lysine + phenazine methosulfate
6-amino-2-oxohexanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-lysine + phenazine methosulfate
6-amino-2-oxohexanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-Met + H2O + oxidized 2,6-dichlorophenolindophenol
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
0.8% activity compared to D-Pro
-
-
?
D-Met + H2O + oxidized 2,6-dichlorophenolindophenol
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
0.8% activity compared to D-Pro
-
-
?
D-methionine + phenazine methosulfate
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-methionine + phenazine methosulfate
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced phenazine methosulfate
-
overall reaction
-
?
D-phenylalanine + H2O + 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-phenylalanine + H2O + 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-Pro + H2O + coenzyme Q1
?
D-Pro is the best substrate
-
-
?
D-serine + H2O + 2,6-dichlorophenolindophenol
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-serine + H2O + 2,6-dichlorophenolindophenol
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
low activity
-
?
additional information
?
-
no substrates: aspartae, glutamate
-
-
-
additional information
?
-
no substrates: aspartae, glutamate
-
-
-
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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
D-alanine + H2O + FAD
pyruvate + NH3 + FADH2
D-amino acid dehydrogenase activity of broad substrate specificity
-
-
?
D-Pro + H2O + coenzyme Q1
?
D-Pro is the best substrate
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
mutant Y249F protein shows both an active yellow FAD (Y249F-y) and an inactive chemically modified green 6-hydroxy-FAD cofactor. Variants show no differences in the overall protein structure and fold. Variant Y249F-y displays an alternative conformation for some active site residues and the flavin cofactor. Y249F-y with FAD samples a metastable conformational state, not available to the wild-type enzyme. The alternate conformation in the Y249F-y enzyme is responsible for the higher spin density at the C6 atom of flavin, consistent with the formation of 6-hydroxy-FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
inhibition of the dichlorophenolindophenol-specific enzyme at high concentrations
benzoic acid
0.1 mM, 98% inhibition
D-Amino acids
-
various D-amino acids competitively inhibit D-kynurenine deamination
p-chloromercuribenzoic acid
-
90% inhibition of the methylene blue specific, 70% inhibition of the dichlorophenolindophenol specific enzyme at 0.5 mM
p-hydroxymercuribenzoate
0.1 mM, 78.6% inhibition
iodoacetamide
0.1 mM, 65.8% inhibition
iodoacetate
0.1 mM, 61.8% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
histidine triad nucleotide binding protein 1
-
catalytically active histidine triad nucleotide binding protein 1 is necessary for enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
alanine racemase deficiency
Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of D-amino acid dehydrogenase and the catabolic alanine racemase.
Scrapie
Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
2,6-dichlorophenolindophenol
-
specific acceptor, cosubstrate: D-kynurenine
0.0082
coenzyme Q1
in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.45
D-kynurenine
-
both methylene blue and 2,6-dichlorophenolindophenol specific enzymes
40.2
D-Pro
with Q1 as the electron acceptor, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.47
D-tryptophan
-
both methylene blue and 2,6-dichlorophenolindophenol specific enzymes