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Enzyme Nomenclature
Information on EC 1.4.5.1 - D-amino acid dehydrogenase (quinone)
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EC Tree
1.4.5.1 D-amino acid dehydrogenase (quinone)IUBMB Comments
An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DadA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a D-amino acid + H2O + a quinone = a 2-oxo carboxylate + NH3 + a quinol
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
D-amino acid:quinone oxidoreductase (deaminating)
An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6.
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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
beta-chloro-D-alanine + oxidized acceptor + H2O
? + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 20% of the activity with D-alanine
-
-
?
D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol
D-Ala + oxidized coenzyme Q1 + H2O
pyruvate + NH3 + reduced coenzyme Q1
specific activity is 37% of that with D-proline
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
D-alanine + oxidized 2,6-dichlorophenolindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichlorophenolindophenol
-
r
-
-
?
D-alanine + oxidized acceptor
pyruvate + NH3 + reduced acceptor
-
the enzyme couples D-alanine oxidation to solute active transport in Escherichia coli B cytoplasmic membrane vesicles
-
-
?
D-alanine + oxidized coenzyme Q1
pyruvate + NH3 + reduced coenzyme Q1
-
no activity with menaquinone or adriamycin
-
-
?
D-arginine + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxo-5-guanidinopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
41% of the activity with D-alanine
-
-
?
D-arginine + oxidized acceptor + H2O
2-oxo-5-guanidinopentanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 2.9% of the activity with D-alanine
-
-
?
D-asparagine + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxosuccinamic acid + NH3 + reduced 2,6-dichlorophenolindophenol
D-asparagine + oxidized acceptor + H2O
2-oxosuccinamic acid + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 21% of the activity with D-alanine
-
-
?
D-cycloserine + oxidized 2,6-dichloroindophenol + H2O
?
-
as a active as D-alanine
-
-
?
D-cysteine + oxidized acceptor
? + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 4.1% of the activity with D-alanine
-
-
?
D-ethionine + oxidized acceptor + H2O
? + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 41% of the activity with D-alanine
-
-
?
D-glutamine + oxidized 2,6-dichloroindophenol + H2O
4-carbamoyl-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
D-histidine + oxidized 2,6-dichloroindophenol + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
-
8.5% of the activity compared to D-alanine
-
-
?
D-histidine + oxidized acceptor + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 12% of the activity with D-alanine
-
-
?
D-leucine + oxidized acceptor + H2O
4-methyl-2-oxopentanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 20% of the activity with D-alanine
-
-
?
D-methionine + oxidized 2,6-dichloroindophenol + H2O
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
D-methionine + oxidized 2,6-dichlorophenolindophenol + H2O
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
70% of the activity with D-alanine
-
-
?
D-methionine + oxidized acceptor + H2O
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 39% of the activity with D-alanine
-
-
?
D-Phe + oxidized coenzyme Q1 + H2O
phenylpyruvate + NH3 + reduced coenzyme Q1
specific activity is 20% of that with D-proline
-
-
?
D-phenylalanine + oxidized 2,6-dichloroindophenol + H2O
phenylpyruvate + NH3 + reduced 2,6-dichloroindophenol
D-phenylalanine + oxidized acceptor + H2O
phenylpyruvate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 72% of the activity with D-alanine
-
-
?
D-proline + oxidized 2,6-dichloroindophenol
DELTA1-pyrroline-2-carboxylate + reduced 2,6-dichloroindophenol
-
28% of the activity compared to D-alanine
-
-
?
D-proline + oxidized 2,6-dichlorophenolindophenol
DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol
-
19% of the activity with D-alanine
-
-
?
D-proline + oxidized acceptor
DELTA1-pyrroline-2-carboxylate + reduced acceptor
-
assayed in toluenized cells, reaction rate is 2.6% of the activity with D-alanine
-
-
?
D-proline + oxidized coenzyme Q1 + H2O
DELTA1-pyrroline-2-carboxylate + NH3 + reduced coenzyme Q1
-
-
-
?
D-Ser + oxidized coenzyme Q1 + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced coenzyme Q1
specific activity is 7% of that with D-proline
-
-
?
D-serine + oxidized 2,6-dichloroindophenol + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol
-
29% of the activity compared to D-alanine
-
-
?
D-serine + oxidized 2,6-dichlorophenolindophenol + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
20% of the activity compared to D-alanine
-
-
?
D-serine + oxidized acceptor + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 13% of the activity with D-alanine
-
-
?
D-threonine + H2O + oxidized acceptor
3-hydroxy-2-oxobutanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 5.9% of the activity with D-alanine
-
-
?
D-valine + oxidized 2,6-dichloroindophenol + H2O
2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol
-
11% of the activity compared to D-alanine
-
-
?
D-valine + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol
-
26% of the activity with D-alanine
-
-
?
D-valine + oxidized acceptor + H2O
2-oxoisopentanoate + NH3 + reduced acceptor
-
assayed in toluenized cells, reaction rate is 2.6% of the activity with D-alanine
-
-
?
additional information
?
-
activity with D-Val, D-Met, D-Glu, D-Asp, L-Pro and L-Ala is below 5% of the activity with D-Pro
-
-
?
3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol
?
-
when membrane fractions from Escherichia coli strain UMM5 (putA1::Tn5 proC24) lacking both L-proline dehydrogenase and L-DELTA1-pyrroline-5-carboxylate reductase are incubated with 3,4-dehydro-DL-proline, pyrrole-2-carboxylate is formed. Oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is induced by growth in minimal medium containing D- or L-alanine. An Escherichia coli strain with no D-alanine dehydrogenase activity due to the dadA237 mutation is unable to oxidize either 3,4-dehydro-D-proline or D-alanine, as are spontaneous Dad- mutants of Escherichia coli strain UMM5. Membrane fractions containing D-alanine dehydrogenase also catalyze the oxidation of D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. D-Alanine dehydrogenase is responsible for the residual 3,4-dehydro-DL-proline oxidation activity in putA proC mutants of Escherichia coli. This enzyme plays a general role in the metabolism of D-amino acids and their analogues
-
-
?
3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol
?
-
when membrane fractions from Escherichia coli strain UMM5 (putA1::Tn5 proC24) lacking both L-proline dehydrogenase and L-DELTA1-pyrroline-5-carboxylate reductase are incubated with 3,4-dehydro-DL-proline, pyrrole-2-carboxylate is formed. Oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is induced by growth in minimal medium containing D- or L-alanine. An Escherichia coli strain with no D-alanine dehydrogenase activity due to the dadA237 mutation is unable to oxidize either 3,4-dehydro-D-proline or D-alanine, as are spontaneous Dad- mutants of Escherichia coli strain UMM5. Membrane fractions containing D-alanine dehydrogenase also catalyze the oxidation of D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. D-Alanine dehydrogenase is responsible for the residual 3,4-dehydro-DL-proline oxidation activity in putA proC mutants of Escherichia coli. This enzyme plays a general role in the metabolism of D-amino acids and their analogues
-
-
?
D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol
-
38% of the activity compared to D-alanine
-
-
?
D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol
-
89% of the activity compared to D-alanine
-
-
?
D-2-amino-n-butyrate + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxobutyrate + NH3 + reduced 2,6-dichloroindophenol
-
81% of the activity with D-alanine
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-alanine + oxidized 2,6-dichloroindophenol + H2O
pyruvate + NH3 + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-alanine + oxidized acceptor + H2O
pyruvate + NH3 + reduced acceptor
-
the enzyme is inducible by L-alanine and repressible by glucose
-
-
?
D-alanine + oxidized acceptor + H2O
pyruvate + NH3 + reduced acceptor
-
assayed in toluenized cells, formation of pyruvate is determined using 2,4-dinitrophenylhydrazine
-
-
?
D-asparagine + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxosuccinamic acid + NH3 + reduced 2,6-dichlorophenolindophenol
-
26% of the activity compared to D-alanine
-
-
?
D-asparagine + oxidized 2,6-dichlorophenolindophenol + H2O
2-oxosuccinamic acid + NH3 + reduced 2,6-dichlorophenolindophenol
-
96% of the activity with D-alanine
-
-
?
D-glutamine + oxidized 2,6-dichloroindophenol + H2O
4-carbamoyl-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-glutamine + oxidized 2,6-dichloroindophenol + H2O
4-carbamoyl-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
-
52% of the activity with D-alanine
-
-
?
D-methionine + oxidized 2,6-dichloroindophenol + H2O
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
-
35% of the activity compared to D-alanine
-
-
?
D-methionine + oxidized 2,6-dichloroindophenol + H2O
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced 2,6-dichloroindophenol
-
97% of the activity compared to D-alanine
-
-
?
D-phenylalanine + oxidized 2,6-dichloroindophenol + H2O
phenylpyruvate + NH3 + reduced 2,6-dichloroindophenol
-
as active as D-alanine
-
-
?
D-phenylalanine + oxidized 2,6-dichloroindophenol + H2O
phenylpyruvate + NH3 + reduced 2,6-dichloroindophenol
-
63% of the activity with D-alanine
-
-
?
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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 + oxidized acceptor
pyruvate + NH3 + reduced acceptor
-
the enzyme couples D-alanine oxidation to solute active transport in Escherichia coli B cytoplasmic membrane vesicles
-
-
?
D-alanine + oxidized acceptor + H2O
pyruvate + NH3 + reduced acceptor
-
the enzyme is inducible by L-alanine and repressible by glucose
-
-
?
3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol
?
-
when membrane fractions from Escherichia coli strain UMM5 (putA1::Tn5 proC24) lacking both L-proline dehydrogenase and L-DELTA1-pyrroline-5-carboxylate reductase are incubated with 3,4-dehydro-DL-proline, pyrrole-2-carboxylate is formed. Oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is induced by growth in minimal medium containing D- or L-alanine. An Escherichia coli strain with no D-alanine dehydrogenase activity due to the dadA237 mutation is unable to oxidize either 3,4-dehydro-D-proline or D-alanine, as are spontaneous Dad- mutants of Escherichia coli strain UMM5. Membrane fractions containing D-alanine dehydrogenase also catalyze the oxidation of D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. D-Alanine dehydrogenase is responsible for the residual 3,4-dehydro-DL-proline oxidation activity in putA proC mutants of Escherichia coli. This enzyme plays a general role in the metabolism of D-amino acids and their analogues
-
-
?
3,4-dehydro-DL-proline + oxidized 2,6-dichloroindophenol
?
-
when membrane fractions from Escherichia coli strain UMM5 (putA1::Tn5 proC24) lacking both L-proline dehydrogenase and L-DELTA1-pyrroline-5-carboxylate reductase are incubated with 3,4-dehydro-DL-proline, pyrrole-2-carboxylate is formed. Oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is induced by growth in minimal medium containing D- or L-alanine. An Escherichia coli strain with no D-alanine dehydrogenase activity due to the dadA237 mutation is unable to oxidize either 3,4-dehydro-D-proline or D-alanine, as are spontaneous Dad- mutants of Escherichia coli strain UMM5. Membrane fractions containing D-alanine dehydrogenase also catalyze the oxidation of D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. D-Alanine dehydrogenase is responsible for the residual 3,4-dehydro-DL-proline oxidation activity in putA proC mutants of Escherichia coli. This enzyme plays a general role in the metabolism of D-amino acids and their analogues
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ubiquinone
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol fold
ubiquinone-0
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 16fold
ubiquinone-1
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 25fold
ubiquinone-2
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 26fold
ubiquinone-3
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 21fold
ubiquinone-4
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 3fold
ubiquinone-5
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 2fold
ubiquinone-6
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 2fold
ubiquinone-7
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 2fold
ubiquinone-8
-
0.2 mM quinone stimulates reaction with D-alanine and oxidized 2,6-dichloroindophenol 2fold
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Mg2+ and Ca2+ have no effect on DadA activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-alanine
-
oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 is competitively inhibited by D-alanine
additional information
EDTA, Mg2+ and Ca2+ have no effect on DadA activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
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
9
-
oxidation of 3,4-dehydro-DL-proline by membrane fractions from strain UMM5 has a pH optimum of 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.5
pH 7.5: about 50% of maximal activity, pH 8.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
25°C: about 50% of maximal activity, 55°C: about 65% of maximal activity
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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). DADA_HELPJ
Helicobacter pylori (strain J99 / ATCC 700824)
410
0
46102
Swiss-Prot
-
DADA_HELPY
Helicobacter pylori (strain ATCC 700392 / 26695)
410
0
46113
Swiss-Prot
-
A0A644U755_9ZZZZ
423
0
44602
TrEMBL
other Location (Reliability: 3)
A0A221K7J7_9RHOB
406
0
44050
TrEMBL
-
A0A1Z5JRF6_FISSO
555
0
61465
TrEMBL
Secretory Pathway (Reliability: 2)
A0A221K3L8_9RHOB
412
1
43863
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
42
-
10 min, solubilized enzyme loses 95% of its activity, the native enzyme loses 49% of its activity
additional information
37
-
10 min, the solubilized enzyme loses 90% of initial activity, the native enzyme loses 20% of initial activity
37
-
60 min, solubilized enzyme loses 98% of its initial activity, the native enzyme loses 47% of its activity
additional information
-
integration of the enzyme within the membrane bilayer confers direct protection against thermal denaturation at 37°C
additional information
-
association with the membrane bilayer protects the enzyme against thermal denaturation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
association with the membrane bilayer protects the enzyme against thermal denaturation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.1 M potassium phosphate, pH 7.5, 0.02% Triton X-100, more than 1 mg protein/ml, stable for at least 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jones, H.; Venables, W.A.
Effects of solubilization on some properties of the membrane-bound respiratory enzyme D-amino acid dehydrogenase of Escherichia coli
FEBS Lett.
151
189-192
1983
Escherichia coli
brenda
Olsiewski, P.J.; Kaczorowski, G.J.; Walsh, C.
Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B
J. Biol. Chem.
255
4487-4494
1980
Escherichia coli B
brenda
Tanigawa, M.; Shinohara, T.; Saito, M.; Nishimura, K.; Hasegawa, Y.; Wakabayashi, S.; Ishizuka, M.; Nagata, Y.D
D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637
Amino Acids
38
247-255
2010
Helicobacter pylori (A3KEZ1)
brenda
Magor, A.M.; Venables, W.A.
Solubilization, purification and characterization of D-alanine dehydrogenase from Pseudomonas aeruginosa and effects of solubilization on its properties
Biochimie
69
63-69
1987
Pseudomonas aeruginosa
brenda
Deutch, C.E.
Oxidation of 3,4-dehydro-D-proline and other D-amino acid analogues by D-alanine dehydrogenase from Escherichia coli
FEMS Microbiol. Lett.
238
383-389
2004
Escherichia coli, Escherichia coli UMM5 (putA1::Tn5 proC24)
brenda
Wild, J.; Klopotowski, T.
D-Amino acid dehydrogenase of Escherichia coli K12: positive selection of mutants defective in enzyme activity and localization of the structural gene
Mol. Gen. Genet.
181
373-378
1981
Escherichia coli K-12
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Release 2023.1 (January 2023)
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