Information on EC 1.4.99.6 - D-arginine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.4.99.6
-
RECOMMENDED NAME
GeneOntology No.
D-arginine dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor
show the reaction diagram
a flavoprotein, FAD; A flavoprotein, FAD. Acts to some extent on all D-amino acids, except D-aspartate and D-glutamate; overall reaction
-
-
-
D-arginine + acceptor = iminoarginine + reduced acceptor
show the reaction diagram
(1a)
-
-
-
iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3
show the reaction diagram
(1b), spontaneous
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-Arginine and D-ornithine metabolism
-
-
Metabolic pathways
-
-
alanine metabolism
-
-
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, is a catabolic enzyme that is part of 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.
CAS REGISTRY NUMBER
COMMENTARY hide
37205-44-0
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3S,3R)-2-oxo-3-methylvaleric acid + NH3 + NADPH + H+
D-isoleucine + H2O + NADP+
show the reaction diagram
2-oxo-3-methylbutyric acid + NH3 + NADPH + H+
D-valine + H2O + NADP+
show the reaction diagram
2-oxo-4-methylvaleric acid + NH3 + NADPH + H+
D-leucine + H2O + NADP+
show the reaction diagram
D-Ala + H2O + FAD
pyruvate + NH3 + FADH2
show the reaction diagram
-
100% activity
-
-
?
D-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-alanine + H2O + 2,6-dichlorophenolindophenol
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-alanine + H2O + methylene blue
pyruvate + NH3 + reduced methylene blue
show the reaction diagram
-
low activity
-
?
D-Arg + H2O + FAD
5-guanidine-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
-
82% activity compared to D-Ala
-
-
?
D-arginine + H2O + iodonitrotetrazolium chloride
5-guanidino-2-oxopentanoate + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
D-arginine and D-lysine are the most effective substrates
-
-
?
D-arginine + phenazine methosulfate
5-guanidino-2-oxopentanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
D-Asn + H2O + FAD
2-oxosuccinamic acid + NH3 + H2O2
show the reaction diagram
-
37% activity compared to D-Ala
-
-
?
D-Asp + H2O + FAD
2-oxobutanedioate + NH3 + H2O2
show the reaction diagram
-
34% activity compared to D-Ala
-
-
?
D-Asp + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxobutanedioate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-asparagine + H2O + 2,6-dichlorophenolindophenol
2-oxosuccinamic acid + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-asparagine + H2O + methylene blue
2-oxosuccinamic acid + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-cysteine + H2O + methylene blue
3-mercapto-2-oxopropanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-cystine + H2O + methylene blue
? + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-Gln + H2O + FAD
2-oxoglutaramate + NH3 + H2O2
show the reaction diagram
-
4% activity compared to D-Ala
-
-
?
D-Glu + H2O + FAD
2-oxoglutarate + NH3 + H2O2
show the reaction diagram
-
3% activity compared to D-Ala
-
-
?
D-Glu + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxoglutarate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-His + H2O + FAD
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
show the reaction diagram
-
60% activity compared to D-Ala
-
-
?
D-histidine + H2O + 2,6-dichlorophenolindophenol
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-histidine + H2O + iodonitrotetrazolium chloride
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
-
-
-
?
D-histidine + H2O + methylene blue
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-histidine + phenazine methosulfate
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
D-isoleucine + H2O + 2,6-dichlorophenolindophenol
3-methyl-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-isoleucine + H2O + methylene blue
3-methyl-2-oxopentanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-kynurenine + H2O + 2,6-dichlorophenolindophenol
4-(2-aminophenyl)-2,4-dioxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-kynurenine + H2O + methylene blue
4-(2-aminophenyl)-2,4-dioxobutanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-Leu + H2O + FAD
4-methyl-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
-
60% activity compared to D-Ala
-
-
?
D-leucine + H2O + 2,6-dichlorophenolindophenol
4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-leucine + H2O + methylene blue
4-methyl-2-oxopentanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-leucine + phenazine methosulfate
? + NH3 + reduced phenazine methosulfate
show the reaction diagram
D-Lys + H2O + FAD
4-amino-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
-
59% activity compared to D-Ala
-
-
?
D-lysine + H2O + iodonitrotetrazolium chloride
7-amino-2-oxoheptanoic acid + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
D-arginine and D-lysine are the most effective substrates
-
-
?
D-lysine + phenazine methosulfate
6-amino-2-oxohexanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
D-Met + H2O + FAD
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram
-
83% activity compared to D-Ala
-
-
?
D-Met + H2O + oxidized 2,6-dichlorophenolindophenol
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-methionine + H2O + 2,6-dichlorophenolindophenol
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-methionine + H2O + iodonitrotetrazolium chloride
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
-
-
-
?
D-methionine + phenazine methosulfate
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
D-norleucine + H2O + 2,6-dichlorophenolindophenol
2-oxohexanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-norleucine + H2O + methylene blue
2-oxohexanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-norvaline + H2O + methylene blue
2-oxopentanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-Orn + H2O + FAD
5-amino-2-oxopentanoate + NH3 + H2O2
show the reaction diagram
-
65% activity compared to D-Ala
-
-
?
D-ornithine + H2O + iodonitrotetrazolium chloride
? + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
-
-
-
?
D-Phe + H2O + FAD
phenylpyruvate + NH3 + H2O2
show the reaction diagram
-
81% activity compared to D-Ala
-
-
?
D-Phe + H2O + oxidized 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
19.8% activity compared to D-Pro
-
-
?
D-phenylalanine + H2O + 2,6-dichlorophenolindophenol
phenylpyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-phenylalanine + H2O + iodonitrotetrazolium chloride
phenylpyruvate + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
-
-
-
?
D-phenylalanine + H2O + methylene blue
phenylpyruvate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-phenylalanine + phenazine methosulfate
2-oxo-3-phenylpropanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
-
-
overall reaction
-
?
D-Pro + H2O + coenzyme Q1
?
show the reaction diagram
D-Pro + H2O + FAD
?
show the reaction diagram
-
104% activity compared to D-Ala
-
-
?
D-Pro + H2O + oxidized 2,6-dichlorophenolindophenol
DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
100% activity
-
-
?
D-proline + H2O + 2,6-dichlorophenolindophenol
DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-proline + H2O + coenzyme Q1
DELTA1-pyrroline-2-carboxylate + NH3 + reduced coenzyme Q1
show the reaction diagram
-
-
-
?
D-Ser + H2O + FAD
3-hydroxy-2-oxopropanoate + NH3 + H2O2
show the reaction diagram
-
67% activity compared to D-Ala
-
-
?
D-Ser + H2O + oxidized 2,6-dichlorophenolindophenol
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
6.7% activity compared to D-Pro
-
-
?
D-serine + H2O + 2,6-dichlorophenolindophenol
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-serine + H2O + methylene blue
3-hydroxy-2-oxopropanoate + NH3 + reduced methylene blue
show the reaction diagram
-
low activity
-
?
D-Thr + H2O + FAD
3-hydroxy-2-oxobutanoate + NH3 + H2O2
show the reaction diagram
-
34% activity compared to D-Ala
-
-
?
D-threonine + H2O + 2,6-dichlorophenolindophenol
3-hydroxy-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
low activity
-
?
D-threonine + H2O + methylene blue
3-hydroxy-2-oxobutanoate + NH3 + reduced methylene blue
show the reaction diagram
-
low activity
-
?
D-Trp + H2O + FAD
3-indole-2-oxopropanoate + NH3 + FADH2
show the reaction diagram
-
37% activity compared to D-Ala
-
-
?
D-tryptophan + H2O + 2,6-dichlorophenolindophenol
3-indole-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-tryptophan + H2O + methylene blue
3-indole-2-oxopropanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-Tyr + H2O + FAD
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + H2O2
show the reaction diagram
-
150% activity compared to D-Ala
-
-
?
D-tyrosine + H2O + 2,6-dichlorophenolindophenol
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-tyrosine + H2O + iodonitrotetrazolium chloride
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced iodonitrotetrazolium chloride
show the reaction diagram
-
-
-
-
?
D-tyrosine + H2O + methylene blue
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
D-tyrosine + phenazine methosulfate
3-(4-hydroxyphenyl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
-
-
overall reaction
-
?
D-Val + H2O + FAD
3-methyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram
-
47% activity compared to D-Ala
-
-
?
D-Val + H2O + oxidized 2,6-dichlorophenolindophenol
2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
0.8% activity compared to D-Pro
-
-
?
D-valine + H2O + 2,6-dichlorophenolindophenol
2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
D-valine + H2O + methylene blue
2-oxoisopentanoate + NH3 + reduced methylene blue
show the reaction diagram
-
-
-
?
L-Ala + H2O + oxidized 2,6-dichlorophenolindophenol
?
show the reaction diagram
1.9% activity compared to D-Pro
-
-
?
L-Pro + H2O + oxidized 2,6-dichlorophenolindophenol
?
show the reaction diagram
3.5% activity compared to D-Pro
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Pro + H2O + coenzyme Q1
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
the yield is highest in the presence of 0.5 mM NADP+
NADPH
-
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
not influenced by Mg2+ and Ca+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
inhibition of the dichlorophenolindophenol-specific enzyme at high concentrations
4-hydroxybenzoic acid
21.4% residual activity at 0.1 mM
Benzoate
2% residual activity at 0.1 mM
D-Amino acids
-
various D-amino acids competitively inhibit D-kynurenine deamination
D-arginine
-
substrate inhibition
D-Lysine
-
substrate inhibition
iodoacetamide
iodoacetate
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
additional information
not inhibited by EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histidine triad nucleotide binding protein 1
-
catalytically active histidine triad nucleotide binding protein 1 is necessary for enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
2,6-dichlorophenolindophenol
-
specific acceptor, cosubstrate: D-kynurenine
32.3
2-oxo-4-methylvaleric acid
-
at pH 10.5 and 50°C
0.0082
coenzyme Q1
in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.46
D-Ala
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
5.37
D-Arg
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
0.06 - 0.36
D-arginine
0.81
D-His
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
3.52 - 11
D-histidine
0.45
D-kynurenine
-
both methylene blue and 2,6-dichlorophenolindophenol specific enzymes
1.8 - 12
D-Leucine
0.19 - 0.26
D-Lysine
1.43 - 10
D-methionine
1.48
D-ornithine
-
-
1.07
D-Phe
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
1.13 - 11
D-phenylalanine
1.82 - 40.2
D-Pro
0.0082 - 40.2
D-proline
1.65
D-Ser
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
2.47
D-Thr
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
0.47
D-tryptophan
-
both methylene blue and 2,6-dichlorophenolindophenol specific enzymes
1.78
D-Tyr
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
0.4 - 0.8
D-tyrosine
3.01
D-Val
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
0.008
methylene blue
-
specific acceptor, cosubstrate: D-kynurenine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5700
2-oxo-4-methylvaleric acid
Ureibacillus thermosphaericus
-
at pH 10.5 and 50°C
0.74
D-Ala
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
1.27
D-Arg
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
11.1 - 420
D-arginine
0.84
D-His
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
3.6 - 35
D-histidine
0.061 - 55
D-Leucine
9.2 - 550
D-Lysine
6.8 - 190
D-methionine
6.2
D-ornithine
Pseudomonas aeruginosa
-
-
1.1
D-Phe
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
5.3 - 75
D-phenylalanine
0.97
D-Pro
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
0.8
D-Ser
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
0.68
D-Thr
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
1.1
D-Tyr
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
3.6 - 23
D-tyrosine
0.78
D-Val
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
180
2-oxo-4-methylvaleric acid
Ureibacillus thermosphaericus
-
at pH 10.5 and 50°C
19410
1.61
D-Ala
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
291
0.236
D-Arg
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
1349
140 - 3400
D-arginine
1255
1.04
D-His
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
3625
1 - 4
D-histidine
3068
0.033 - 12
D-Leucine
2480
48 - 580
D-Lysine
1531
4.8 - 36
D-methionine
957
4.2
D-ornithine
Pseudomonas aeruginosa
-
-
2550
1.03
D-Phe
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
946
4.7 - 6.9
D-phenylalanine
1232
0.533
D-Pro
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
1864
0.485
D-Ser
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
972
0.275
D-Thr
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
2991
0.618
D-Tyr
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
2139
9.1 - 27.6
D-tyrosine
1643
0.259
D-Val
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl (pH 8.7), at 37°C
2157
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.1
D-arginine
-
-
150
D-Lysine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
purified enzyme, with 20 mM D-Asp as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C; purified enzyme, with 20 mM D-Met as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C; purified enzyme, with 20 mM D-Val as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.06
purified enzyme, with 20 mM D-Glu as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.113
-
methylene blue specific enzyme
0.12
purified enzyme, with 20 mM L-Ala as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.213
-
2,6-dichlorophenolindophenol specific enzyme
0.22
purified enzyme, with 20 mM L-Pro as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
0.46
cell-free extract, with 20 mM D-Pro as the substrate, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
both methylene blue and 2,6-dichlorophenolindophenol specific enzymes
10.5
-
pH-optimum for D-leucine synthesisin glycine-KOH buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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temperature optimum for D-leucine synthesis
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
one methylene blue specific, one 2,6-dichlorophenolindophenol specific enzyme, the methylene blue specific enzyme is only detectable in D-tryptophan grown cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
4 * 20000, SDS-PAGE
46040
x * 46040, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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4 * 20000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with D-leucine, to 1.07 A resolution. Structure reveals a covalent N(5) flavin adduct, instead of the expected iminoleucine product in the active site. This acyl adduct can be reproduced by photoreduction of the enzyme in the presence of 4-methyl-2-oxopentanoic acid (ketoleucine)
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in complex with iminoarginine, to 1.06 A resolution, and in complex with iminohistidine, to 1.3 A resolution. The structure comprises an unliganded conformation and a product-bound conformation. The active site is partially occupied with iminoarginine product that interacts with Tyr53 in the minor conformation of a surface loop. The guanidinium side chain of iminoarginine forms a hydrogen bond interaction with the hydroxyl of Thr50 and an ionic interaction with Glu87. In complex with iminohistidine, two alternate conformations are observed for iminohistidine where the imidazole groups form hydrogen bond interactions with the side chains of His48 and Thr50 and either Glu87 or Gln336. The different interactions and very distinct binding modes observed for iminoarginine and iminohistidine are consistent with the 1000fold difference in kcat/Km values for D-arginine and D-histidine
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography
HisTrap column chromatography
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near homogeneity, two enzymes with different acceptor specificities, fractionation and chromatography techniques
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Sepharose column chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH10B cells
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expressed in Escherichia coli Rosetta (DE3) cells
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expressed in Escherichia coli Top10 cells
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recombinantly expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of dauBAR is specifically induced by exogenous D-arginine and D-lysine
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the dadA promoter is induced by several L-amino acids, most strongly by Ala, and only by D-Ala among all tested D-amino acids
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E87L
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kcat/Km pH-profile of the E87L mutant indicates only a single unprotonated group is required for maximal activity with D-arginine. E87 is the unprotonated group on the enzyme that binds cationic substrates
H48F
-
residue H48 is not responsible for the observed pKa value
Y249F
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steady-state kinetic parameters similar to those of the wild-type enzyme. Rate constants for flavin reduction (kred) with D-leucine are 3fold smaller than the wild-type value with similar pKa values for an unprotonated group of about 10.0. Cleavage of the substrate NH and CH bonds in the enzyme variant occurs in synchronous fashion, which can be reconciled with a hydride transfer mechanism
Y53F
-
steady-state kinetic parameters similar to those of the wild-type enzyme. Rate constants for flavin reduction (kred) with D-leucineare 3fold smaller than the wild-type value with similar pKa values for an unprotonated group of about 10.0. Cleavage of the substrate NH and CH bonds in the enzyme variant occurs in synchronous fashion, which can be reconciled with a hydride transfer mechanism
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