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D-alanine + phenazine methosulfate + H2O
pyruvate + NH3 + reduced phenazine methosulfate
-
-
-
?
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-asparagine + phenazine methosulfate + H2O
2-oxobutanedioate + 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
D-histidine + phenazine methosulfate + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-isoleucine + phenazine methosulfate + H2O
3-methyl-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-leucine + phenazine methosulfate
? + NH3 + reduced phenazine methosulfate
D-leucine + phenazine methosulfate + H2O
4-methyl-2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
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-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-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-proline + phenazine methosulfate + H2O
DELTA1-pyrroline-2-carboxylate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-serine + phenazine methosulfate + H2O
3-hydroxy-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-threonine + phenazine methosulfate + H2O
3-hydroxy-2-oxobutanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-tryptophan + phenazine methosulfate + H2O
3-indole-2-oxopropanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
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-valine + phenazine methosulfate + H2O
2-oxopentanoate + NH3 + reduced phenazine methosulfate
-
-
-
?
D-alanine + H2O + FAD
pyruvate + NH3 + FADH2
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-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-lysine + H2O + iodonitrotetrazolium chloride
7-amino-2-oxoheptanoic acid + NH3 + reduced iodonitrotetrazolium chloride
-
D-arginine and D-lysine are the most effective substrates
-
-
?
D-methionine + H2O + iodonitrotetrazolium chloride
4-methylsulfanyl-2-oxobutanoate + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
D-ornithine + H2O + iodonitrotetrazolium chloride
? + NH3 + reduced iodonitrotetrazolium chloride
-
-
-
-
?
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-proline + H2O + FAD
2-oxopentanoic acid + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-serine + H2O + FAD
3-hydroxy-2-oxopropanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
D-threonine + H2O + FAD
3-hydroxy-2-oxobutanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
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-valine + H2O + FAD
2-oxopentanoate + NH3 + FADH2
the enzyme is an efficient D-amino acid dehydrogenase of broad substrate specificity
-
-
?
additional information
?
-
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-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-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-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
-
-
?
additional information
?
-
no substrates: aspartae, glutamate
-
-
-
additional information
?
-
-
no substrates: aspartae, glutamate
-
-
-
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Li, C.; Yao, X.; Lu, C.D.
Regulation of the dauBAR Operon and Characterization of D-Amino Acid Dehydrogenase DauA in Arginine and Lysine Catabolism of Pseudomonas aeruginosa PAO1
Microbiology
156
60-71
2009
Pseudomonas aeruginosa
brenda
Li, C.; Lu, C.D.
Arginine racemization by coupled catabolic and anabolic dehydrogenases
Proc. Natl. Acad. Sci. USA
106
906-911
2009
Pseudomonas aeruginosa (Q9HXE3)
brenda
Oliver, K.E.; Silo-Suh, L.
Impact of D-amino acid dehydrogenase on virulence factor production by a Pseudomonas aeruginosa
Can. J. Microbiol.
59
598-603
2013
Pseudomonas aeruginosa
brenda
Ball, J.; Bui, Q.V.; Gannavaram, S.; Gadda, G.
Importance of glutamate 87 and the substrate alpha-amine for the reaction catalyzed by D-arginine dehydrogenase
Arch. Biochem. Biophys.
568
56-63
2015
Pseudomonas aeruginosa (Q9HXE3)
brenda
Fu, G.; Yuan, H.; Li, C.; Lu, C.D.; Gadda, G.; Weber, I.T.
Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase
Biochemistry
49
8535-8545
2010
Pseudomonas aeruginosa (Q9HXE3), Pseudomonas aeruginosa
brenda
Yuan, H.; Fu, G.; Brooks, P.T.; Weber, I.; Gadda, G.
Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa
Biochemistry
49
9542-9550
2010
Pseudomonas aeruginosa (Q9HXE3), Pseudomonas aeruginosa
brenda
Fu, G.; Yuan, H.; Wang, S.; Gadda, G.; Weber, I.T.
Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase
Biochemistry
50
6292-6294
2011
Pseudomonas aeruginosa (Q9HXE3)
brenda
Gannavaram, S.; Sirin, S.; Sherman, W.; Gadda, G.
Mechanistic and computational studies of the reductive half-reaction of tyrosine to phenylalanine active site variants of D-arginine dehydrogenase
Biochemistry
53
6574-6583
2014
Pseudomonas aeruginosa (Q9HXE3), Pseudomonas aeruginosa
brenda
Yuan, H.; Xin, Y.; Hamelberg, D.; Gadda, G.
Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects
J. Am. Chem. Soc.
133
18957-18965
2011
Pseudomonas aeruginosa (Q9HXE3)
brenda
Ouedraogo, D.; Souffrant, M.; Vasquez, S.; Hamelberg, D.; Gadda, G.
Importance of loop L1 dynamics for substrate capture and catalysis in Pseudomonas aeruginosa D-arginine dehydrogenase
Biochemistry
56
2477-2487
2017
Pseudomonas aeruginosa (Q9HXE3), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9HXE3)
brenda
He, W.; Li, C.; Lu, C.-D.
Regulation and characterization of the dadRAX locus for D-amino acid catabolism in Pseudomonas aeruginosa PAO1
J. Bacteriol.
193
2107-2115
2011
Pseudomonas aeruginosa (Q9HTQ0), Pseudomonas aeruginosa
brenda
Hodge-Hanson, K.M.; Downs, D.M.
Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro
PLoS ONE
12
e0185544
2017
Pseudomonas aeruginosa
brenda
Ouedraogo, D.; Ball, J.; Iyer, A.; Reis, R.A.G.; Vodovoz, M.; Gadda, G.
Amine oxidation by D-arginine dehydrogenase in Pseudomonas aeruginosa
Arch. Biochem. Biophys.
632
192-201
2017
Pseudomonas aeruginosa (Q9HXE3), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9HXE3)
brenda
Iyer, A.; Reis, R.A.G.; Gannavaram, S.; Momin, M.; Spring-Connell, A.M.; Orozco-Gonzalez, Y.; Agniswamy, J.; Hamelberg, D.; Weber, I.T.; Gozem, S.; Wang, S.; Germann, M.W.; Gadda, G.
A single-point mutation in D-arginine dehydrogenase unlocks a transient conformational state resulting in altered cofactor reactivity
Biochemistry
60
711-724
2021
Pseudomonas aeruginosa (Q9HXE3)
brenda