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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
L-serine:NAD oxidoreductase (deaminating), NAD+-dependent L-serine dehydrogenase, protein PA0743, serine dehydrogenase,
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L-serine:NAD oxidoreductase (deaminating)
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NAD+-dependent L-serine dehydrogenase
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serine dehydrogenase
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L-serine + H2O + NAD+ = 3-hydroxypyruvate + NH3 + NADH + H+
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oxidative deamination
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reductive amination redox reaction
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L-serine:NAD+ 2-oxidoreductase (deaminating)
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(R)-3-hydroxyisobutyric acid + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
(S)-3-hydroxyisobutyric acid + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
3-methyl-DL-serine + H2O + NAD+
2-aminomethylmalonate semialdehyde + NH3 + NADH + H+
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high activity
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?
D-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + H+
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low activity
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?
DL-glycerate + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
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?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + H+
methyl (R)-3-hydroxy-2-methylpropionic acid + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
methyl (S)-3-hydroxy-2-methylpropionic acid + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
methyl 2,2-dimethyl-3-hydroxypropionic acid + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
tert-butyl 3-hydroxypropionic acid + H2O + NAD+
? + NH3 + NADH + H+
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low activity
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?
additional information
?
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L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + H+
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?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + H+
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best substrate
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?
additional information
?
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no substrates in presence of NADH: alpha-ketoglutarate, oxaloacetate, glyoxylate, or pyruvate
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?
additional information
?
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PA0743 from Pseudomonas aeruginosa catalyzes NAD-dependent oxidation of L-serine and methyl-L-serine, and exhibits low activity against beta-hydroxyisobutyrate
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?
additional information
?
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substrate specificity, overview. No activity with (S)-beta-hydroxybutyric acid, (R)-3-hydroxybutyric acid, 2-hydroxyisobutyric acid, methyl-2-hydroxyisobutyric acid, ethyl-2-hydroxyisobutyric acid, 2-hydroxybutyric acid, DL-malic acid, and DL-homoserine
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?
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L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
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?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + H+
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?
additional information
?
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PA0743 from Pseudomonas aeruginosa catalyzes NAD-dependent oxidation of L-serine and methyl-L-serine, and exhibits low activity against beta-hydroxyisobutyrate
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?
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NAD+
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binding GLGXMG motif-1 and motif-4, the nicotinamide moiety of NAD+ is mostly buried in the interdomain cleft of the PA0743 protomer
NADH
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specific for NADH, does not react with NADPH, strictly specific for hydroxypyruvate in presence of NADH
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p-chloromercurybenzoate
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completely inhibited at 0.005 mM
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2.4
3-methyl-DL-serine
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
19.8
DL-glycerate
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
0.0005
Hydroxypyruvate
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2.5
L-serine
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
17.4
methyl 2,2-dimethyl-3-hydroxypropionic acid
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
3.4
NAD+
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
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9.6
3-methyl-DL-serine
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
5.8
DL-glycerate
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
10.4
L-serine
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
11.6
methyl 2,2-dimethyl-3-hydroxypropionic acid
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
1.6
NAD+
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
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40
3-methyl-DL-serine
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
0.3
DL-glycerate
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
40
L-serine
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
0.7
methyl 2,2-dimethyl-3-hydroxypropionic acid
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
0.5
NAD+
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pH 11.0, 37°C, recombinant His-tagged wild-type enzyme
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brenda
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brenda
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green leaves
brenda
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additional information
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the enzyme has an N-terminal Rossmann fold domain connected by a long alpha-helix to the C-terminal all-alpha domain. Critical role of four amino acid residues in catalysis including the primary catalytic residue Lys171, PA0743 substrate-binding site structure and molecular mechanisms of substrate selectivity, overview. The structure of the PA0743-NAD+ complex demonstrates that the opposite side of the enzyme active site accommodates the cofactor, which is also bound near Lys171
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additional information
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the enzyme has an N-terminal Rossmann fold domain connected by a long alpha-helix to the C-terminal all-alpha domain. Critical role of four amino acid residues in catalysis including the primary catalytic residue Lys171, PA0743 substrate-binding site structure, and molecular mechanisms of substrate selectivity, overview. The structure of the PA0743-NAD+ complex demonstrates that the opposite side of the enzyme active site accommodates the cofactor, which is also bound near Lys171, with dinucleotide cofactor binding GLGXMG motif-1, substrate binding DAPVSGG motif-2, catalysis GXXGXGXXXKXXN motif-3, and cofactor binding motif-4
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purified His-tagged recombinant protein PA0743 alone or in complex with cofactor NAD+, hanging drop vapor diffusion method, mixing of 0.002 ml protein solution with 0.002 ml reservoir solution containing 4 M ammonium acetate and 0.1 M sodium acetate, at pH 5.4, 1 week, soaking of crystals in 10 mM NAD+ solution for complexcystals, X-ray diffraction structure determination and analysis at 2.2 A resolution
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D247A
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site-directed mutagenesis, inactive mutant
E122A
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site-directed mutagenesis, the mutant shows alterations in cofactor binding and highly reduced activity compared to the wild-type enzyme
K171A
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site-directed mutagenesis, inactive mutant
K246A
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site-directed mutagenesis, inactive mutant
N175A
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site-directed mutagenesis, the mutant shows alterations in cofactor binding and highly reduced activity compared to the wild-type enzyme
T96A
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site-directed mutagenesis, the mutant shows alterations in cofactor binding and highly reduced activity compared to the wild-type enzyme
W214A
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site-directed mutagenesis, inactive mutant
Y219A
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site-directed mutagenesis, the mutant shows alterations in cofactor binding and highly reduced activity compared to the wild-type enzyme
additional information
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PA0743 deletion (PW2350) strain from a transposon library
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very labile enzyme, loses its activity when exposed to dialysis or weak heating
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isolated from an albumin fraction, purified on Sephadex G-76, subsequently on DEAE-cellulose
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recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) Gold by nickel affinity chromatography and gel filtration
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PA0743 open reading frame, expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3) Gold
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Kretovich, W.L.; Stepanovich, K.M.
The enzyme catalyzing hydroxypyruvate reductive amination
Izv. Akad. Nauk SSSR Ser. Biol.
2
295-301
1966
Petroselinum crispum
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brenda
Tchigvintsev, A.; Singer, A.; Brown, G.; Flick, R.; Evdokimova, E.; Tan, K.; Gonzalez, C.F.; Savchenko, A.; Yakunin, A.F.
Biochemical and structural studies of uncharacterized protein PA0743 from Pseudomonas aeruginosa revealed NAD+-dependent L-serine dehydrogenase
J. Biol. Chem.
287
1874-1883
2012
Pseudomonas aeruginosa
brenda
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1.4.1.7 serine 2-dehydrogenase
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