Any feedback?
No. of entries
Information on EC 1.1.1.276 - serine 3-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.276
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.276 serine 3-dehydrogenase (NADP+)
IUBMB Comments
NAD+ cannot replace NADP+ [cf. EC 1.1.1.387, serine 3-dehydrogenase (NAD+)].
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
show
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
2-aminomalonate semialdehyde = 2-aminoacetaldehyde + CO2
(1b), spontaneous
-
-
-
L-serine + NADP+ = 2-aminomalonate semialdehyde + NADPH + H+
(1a)
-
-
-
L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+
sequential mechanism
-
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+
-
-
-
L-serine + NADP+ = 2-aminoacetaldehyde + CO2 + NADPH + H+
overall reaction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-serine:NADP+ 3-oxidoreductase
NAD+ cannot replace NADP+ [cf. EC 1.1.1.387, serine 3-dehydrogenase (NAD+)].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9038-55-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: 8.7% activity compared to L-serine
Products: -
Products: -
?
2-methyl-DL-serine + NADP+
2-amino-2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 59% activity compared to L-serine
Products: -
Products: -
?
2-methyl-DL-serine + NADP+
2-amino-2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 21% activity compared to L-serine
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH
-
Substrates: 1.6% activity compared to L-serine
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH
-
Substrates: 23% activity compared to L-serine
Products: -
Products: -
?
3-hydroxypropanoate + NADP+
3-oxopropanoate + NADPH
-
Substrates: 13% activity compared to L-serine
Products: -
Products: -
?
D-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
-
Substrates: 1% activity compared to L-serine
Products: -
Products: -
?
D-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
-
Substrates: 12% activity compared to L-serine
Products: -
Products: -
?
D-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 3.5% activity compared to L-serine
Products: -
Products: -
?
D-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 90% activity compared to L-serine
Products: -
Products: -
?
D-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 78% activity compared to L-serine
Products: -
Products: -
?
D-glycerate + NADP+
?
-
Substrates: 12.9% activity compared to L-serine
Products: -
Products: -
?
D-glycerate + NADP+
?
-
Substrates: 48% activity compared to L-serine
Products: -
Products: -
?
D-glycerate + NADP+
?
-
Substrates: 6% activity compared to L-serine
Products: -
Products: -
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: 55.2% activity compared to L-serine
Products: -
Products: -
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: 83% activity compared to L-serine
Products: -
Products: -
?
D-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: 71% activity compared to L-serine
Products: -
Products: -
?
D-threonine + NADP+
D-2-amino-3-oxobutanoic acid + NADPH
-
Substrates: 156% activity compared to L-serine
Products: -
Products: -
?
D-threonine + NADP+
D-2-amino-3-oxobutanoic acid + NADPH
-
Substrates: 478% activity compared to L-serine
Products: -
Products: -
?
L-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
-
Substrates: 9% activity compared to L-serine
Products: -
Products: -
?
L-3-hydroxybutyrate + NADP+
3-oxobutyrate + NADPH
-
Substrates: 85% activity compared to L-serine
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 8.5% activity compared to L-serine
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 96% activity compared to L-serine
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoic acid + NADPH
-
Substrates: 182% activity compared to L-serine
Products: -
Products: -
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: best substrate
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: 137% activity compared to L-serine
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: best substrate
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: 137% activity compared to L-serine
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: best substrate
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: 397% activity compared to L-serine
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: best substrate
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-allo-threonine + NADP+
L-2-amino-3-ketobutyrate + NADPH
-
Substrates: 397% activity compared to L-serine
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
Products: L-2-amino-3-ketobutyrate spontaneously decarboxylates into aminoacetone
?
L-glycerate + NADP+
?
-
Substrates: 11.3% activity compared to L-serine
Products: -
Products: -
?
L-glycerate + NADP+
?
-
Substrates: 28% activity compared to L-serine
Products: -
Products: -
?
L-glycerate + NADP+
?
-
Substrates: 5% activity compared to L-serine
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: enzyme belongs to the short-chain alcohol dehydrogenase family, similar reaction mechanism
Products: 2-aminomalonate semialdehyde spontaneously decarboxylates into 2-aminoacetaldehyde
Products: 2-aminomalonate semialdehyde spontaneously decarboxylates into 2-aminoacetaldehyde
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: best substrate
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: enzyme belongs to the short-chain alcohol dehydrogenase family, similar reaction mechanism
Products: 2-aminomalonate semialdehyde spontaneously decarboxylates into 2-aminoacetaldehyde
Products: 2-aminomalonate semialdehyde spontaneously decarboxylates into 2-aminoacetaldehyde
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-threonine, D-allo-threonine are poor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-threonine, D-allo-threonine are poor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-threonine, D-allo-threonine are poor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-threonine, D-allo-threonine are poor substrates
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
L-serine + NADP+
2-aminomalonate semialdehyde + NADPH
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no effect with Cu2+, Mg2+, Mn2+, Zn2+, Fe2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methylmalonate
-
competitive against L-serine, noncompetitive against NADP+
D-cysteine
-
competitive against L-serine, noncompetitive against NADP+
L-cysteine
-
competitive against L-serine, noncompetitive against NADP+
malonate
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
substrate specificity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
substrate specificity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (492 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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
x * 25000-26600, recombinant enzyme, SDS-PAGE and amino acid sequence determination
tetramer
-
x * 25000-26600, recombinant enzyme, SDS-PAGE and amino acid sequence determination
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from overproducing Escherichia coli, to homogeneity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in Escherichia coli JM109
-
overexpression in Escherichia coli JM109
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, Agrobacterium tumefaciens ICR 1600, Escherichia coli, 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
Escherichia coli, Escherichia coli YdfG, Saccharomyces cerevisiae, Saccharomyces cerevisiae YMR226C
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.276)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
