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Enzyme Nomenclature
Information on EC 1.1.1.276 - serine 3-dehydrogenase (NADP+)
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EC Tree
1.1.1.276 serine 3-dehydrogenase (NADP+)IUBMB Comments
NAD+ cannot replace NADP+ [cf. EC 1.1.1.387, serine 3-dehydrogenase (NAD+)].
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
2-aminomalonate semialdehyde = 2-aminoacetaldehyde + CO2
(1b), spontaneous
-
-
-
L-serine + NADP+ = 2-aminomalonate semialdehyde + NADPH + H+
(1a)
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-
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L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+
sequential mechanism
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L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+
The product 2-aminomalonate semialdehyde is spontaneously converted into 2-aminoacetaldehyde and CO2. NAD+ cannot replace NADP+
-
-
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L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+
overall reaction
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
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redox reaction
-
-
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reduction
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-
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-
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SYSTEMATIC NAME
IUBMB Comments
L-serine:NADP+ 3-oxidoreductase
NAD+ cannot replace NADP+ [cf. EC 1.1.1.387, serine 3-dehydrogenase (NAD+)].
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CAS REGISTRY NUMBER
COMMENTARY
9038-55-5
-
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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
2-methyl-DL-serine + NADP+
2-amino-2-methyl-3-oxopropanoic acid + NADPH
-
8.7% activity compared to L-serine
-
-
?
2-methyl-DL-serine + NADP+
2-amino-2-methyl-3-oxopropanoic acid + NADPH
-
59% activity compared to L-serine
-
-
?
2-methyl-DL-serine + NADP+
2-amino-2-methyl-3-oxopropanoic acid + NADPH
-
21% activity compared to L-serine
-
-
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH
-
1.6% activity compared to L-serine
-
-
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH
-
23% activity compared to L-serine
-
-
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH
-
13% activity compared to L-serine
-
-
?
D-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
-
1% activity compared to L-serine
-
-
?
D-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
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12% activity compared to L-serine
-
-
?
D-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
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3.5% activity compared to L-serine
-
-
?
D-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
90% activity compared to L-serine
-
-
?
D-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
78% activity compared to L-serine
-
-
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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55.2% activity compared to L-serine
-
-
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
83% activity compared to L-serine
-
-
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
83% activity compared to L-serine
-
-
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
71% activity compared to L-serine
-
-
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
71% activity compared to L-serine
-
-
?
D-threonine + NADP+
D-2-amino-3-oxobutanoic acid + NADPH
-
156% activity compared to L-serine
-
-
?
D-threonine + NADP+
D-2-amino-3-oxobutanoic acid + NADPH
-
478% activity compared to L-serine
-
-
?
L-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
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9% activity compared to L-serine
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-
?
L-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
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85% activity compared to L-serine
-
-
?
L-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
8.5% activity compared to L-serine
-
-
?
L-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
96% activity compared to L-serine
-
-
?
L-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
182% activity compared to L-serine
-
-
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
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best substrate
L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
137% activity compared to L-serine
L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
best substrate
L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
397% activity compared to L-serine
L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-glycerate + NADP+
?
-
5% activity compared to L-serine
-
-
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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-
-
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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best substrate
-
-
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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enzyme belongs to the short-chain alcohol dehydrogenase family, similar reaction mechanism
2-aminomalonate semialdehyde spontaneously decarboxylates into 2-aminoacetaldehyde
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
-
-
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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enzyme belongs to the short-chain alcohol dehydrogenase family, similar reaction mechanism
2-aminomalonate semialdehyde spontaneously decarboxylates into 2-aminoacetaldehyde
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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-
-
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?
additional information
?
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no activity with 4-hydroxybutyrate, DL-2-hydroxybutyrate, DL-2-hydroxyisobutyrate, DL-2-hydroxycaproate, DL-2-hydroxyisocaproate, 3-phosphoglycerate, DL-lactate, L-malate, glycollate, glycerol, D-threonine, DL-threo-phenylserine, DL-homoserine, DL-isoserine, L-alanine, beta-alanine, L-aspartate, L-glutamate, L-valine, L-leucine, L-methionine, L-lysine, L-phenylalanine, and glycine
-
-
?
additional information
?
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no activity with DL-homoserine, O-methyl-L-serine, N-acetyl-DL-serine, DL-isoserine, DL-threo-3-phenylserine, malonate, DL-malate, DL-lactate, DL-tartrate, D-gluconate, citrate, isocitrate, glycolate, glycerol
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-
?
additional information
?
-
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L-threonine, D-allo-threonine are poor substrates
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-
?
additional information
?
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no activity with DL-homoserine, O-methyl-L-serine, N-acetyl-DL-serine, DL-isoserine, DL-threo-3-phenylserine, malonate, DL-malate, DL-lactate, DL-tartrate, D-gluconate, citrate, isocitrate, glycolate, glycerol
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-
?
additional information
?
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L-threonine, D-allo-threonine are poor substrates
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-
?
additional information
?
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no activity with DL-homoserine, O-methyl-L-serine, N-acetyl-DL-serine, DL-isoserine, DL-threo-3-phenylserine, malonate, DL-malate, DL-lactate, DL-tartrate, D-gluconate, citrate, isocitrate, glycolate, glycerol
-
-
?
additional information
?
-
-
L-threonine, D-allo-threonine are poor substrates
-
-
?
additional information
?
-
-
no activity with DL-homoserine, O-methyl-L-serine, N-acetyl-DL-serine, DL-isoserine, DL-threo-3-phenylserine, malonate, DL-malate, DL-lactate, DL-tartrate, D-gluconate, citrate, isocitrate, glycolate, glycerol
-
-
?
additional information
?
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L-threonine, D-allo-threonine are poor substrates
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-
?
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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
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
-
-
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
-
-
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no effect with Cu2+, Mg2+, Mn2+, Zn2+, Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methylmalonate
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competitive against L-serine, noncompetitive against NADP+
D-cysteine
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competitive against L-serine, noncompetitive against NADP+
L-cysteine
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competitive against L-serine, noncompetitive against NADP+
malonate
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competitive against L-serine, noncompetitive against NADP+
Tartronate
-
competitive against L-serine, noncompetitive against NADP+
additional information
-
no inhibition by EDTA, sodium arsenate, o-phenethroline, alpha,alpha'-dipyridyl and very slight inhibition by sodium azide
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
substrate specificity
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
substrate specificity
-
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Ki VALUE [mM]
INHIBITOR
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
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (1099 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
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x * 25000-26600, recombinant enzyme, SDS-PAGE and amino acid sequence determination
tetramer
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x * 25000-26600, recombinant enzyme, SDS-PAGE and amino acid sequence determination
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
10 min, 0.1 M potassium phosphate, pH 7.4, 0.01% 2-mercaptoethanol, 10% glycerol, stable
55
-
10 min, 0.1 M potassium phosphate, pH 7.4, 0.01% 2-mercaptoethanol, 10% glycerol, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from overproducing Escherichia coli, to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in Escherichia coli JM109
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overexpression in Escherichia coli JM109
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chowdhury, E.K.; Higuchi, K.; Nagata, S.; Misono, H.
A novel NADP+ dependent serine dehydrogenase from Agrobacterium tumefaciens
Biosci. Biotechnol. Biochem.
61
152-157
1997
Agrobacterium tumefaciens
brenda
Fujisawa, H.; Nagata, S.; Chowdhury, E.K.; Matsumoto, M.; Misono, H.
Cloning and sequencing of the serine dehydrogenase gene from Agrobacterium tumefaciens
Biosci. Biotechnol. Biochem.
66
1137-1139
2002
Agrobacterium tumefaciens, Escherichia coli, Agrobacterium tumefaciens ICR 1600, Escherichia coli JM109
brenda
Fujisawa, H.; Nagata, S.; Misono, H.
Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C)
Biochim. Biophys. Acta
1645
89-94
2003
Saccharomyces cerevisiae, Escherichia coli, Saccharomyces cerevisiae YMR226C, Escherichia coli YdfG
brenda
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Release 2023.1 (January 2023)
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