Information on EC 1.1.1.3 - homoserine dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.1.3
-
RECOMMENDED NAME
GeneOntology No.
homoserine dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Cysteine and methionine metabolism
-
Glycine, serine and threonine metabolism
-
homoserine biosynthesis
-
Lysine biosynthesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
L-homoserine:NAD(P)+ oxidoreductase
The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a multi-functional protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate kinase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AK-HSD-1
O63067, O65027
-
AK-HSDH
-
isoform 1, bifunctional enzyme EC 2.7.2.4/EC 1.1.1.3
AK-HSDH
O81852
-
aspartate kinase-homoserine dehydrogenase
-
-
aspartate kinase-homoserine dehydrogenase
-
bifunctional enzyme EC 2.7.2.4/EC 1.1.1.3
aspartate kinase-homoserine dehydrogenase
O81852
-
aspartokinase-homoserine dehydrogenase I
-
-
HDH
-
-
-
-
hom-1
D8WXQ1, D8WXQ2
-
hom-1
D8WXQ1, D8WXQ2
-
-
homoserine dehydrogenase 1
-
-
homoserine dehydrogenase 1
Lactobacillus plantarum NCIMB 8826
-
-
-
homoserine dehydrogenase 2
-
-
homoserine dehydrogenase 2
Lactobacillus plantarum NCIMB 8826
-
-
-
HSD
-
-
-
-
HSDH
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-13-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity
-
-
Manually annotated by BRENDA team
slightly modified at base 60 c to t, bas 1242 t to g, and base 1403 t to c, the latter modification results in change of Leu468 to Ser; var. Columbia, bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity
TREMBL
Manually annotated by BRENDA team
var. Bensheim showing threonine and methionine prototrophy, bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity, gene akthr2
-
-
Manually annotated by BRENDA team
isoform hom-1
UniProt
Manually annotated by BRENDA team
isoform hom-2
UniProt
Manually annotated by BRENDA team
isoform hom-1
UniProt
Manually annotated by BRENDA team
isoform hom-2
UniProt
Manually annotated by BRENDA team
two isozymes
-
-
Manually annotated by BRENDA team
a methionine-producing strain carrying mutations in the hom and the thrB genes
-
-
Manually annotated by BRENDA team
bifunctional aspartokinase-homoserine dehydrogenase AK-HSD-1
UniProt
Manually annotated by BRENDA team
bifunctional aspartokinase-homoserine dehydrogenase AK-HSD-2
UniProt
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
mutant strain M20-20D and wild-type strain S2207A
-
-
Manually annotated by BRENDA team
also shows aspartase kinase activity
-
-
Manually annotated by BRENDA team
also shows aspartase kinase activity; spinach
-
-
Manually annotated by BRENDA team
strain NRRL 3585, gene hom
UniProt
Manually annotated by BRENDA team
Streptomyces clavuligerus NRRL 3585
strain NRRL 3585, gene hom
UniProt
Manually annotated by BRENDA team
Thermophilic bacterium
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-, D8WXQ1, D8WXQ2
contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
physiological function
-
contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Calmodulin
-
in the presence of above 0.1 mM Ca2+
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.8
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADPH, pH 8.0, 25C
9.68
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADH, pH 8.0, 25C
11.58
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADPH, pH 8.0, 25C
12.98
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADPH, pH 8.0, 25C
19.3
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADH, pH 8.0, 25C
22.58
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADH, pH 8.0, 25C
0.042
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NADP+, pH 8.0, 25C
0.052
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NADP+, pH 8.0, 25C
0.07
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NADP+, pH 8.0, 25C
0.24
-
L-homoserine
-
recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity
0.51
-
L-homoserine
-
recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity
1.43
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NAD+, pH 8.0, 25C
3.3
-
L-homoserine
-
recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity
7
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NAD+, pH 8.0, 25C
10.15
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NAD+, pH 8.0, 25C
24
-
L-homoserine
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.29
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADPH, pH 8.0, 25C
222982
10.39
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADPH, pH 8.0, 25C
222982
16.22
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADH, pH 8.0, 25C
222982
17.02
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADH, pH 8.0, 25C
222982
26.73
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADH, pH 8.0, 25C
222982
28.54
-
L-aspartate 4-semialdehyde
-, O63067, O65027, Q3S3F6
cosubstrate NADPH, pH 8.0, 25C
222982
0.039
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NADP+, pH 8.0, 25C
12256
0.082
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NAD+, pH 8.0, 25C
12256
0.095
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NADP+, pH 8.0, 25C
12256
0.256
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NADP+, pH 8.0, 25C
12256
0.731
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NAD+, pH 8.0, 25C
12256
0.757
-
L-homoserine
-, O63067, O65027, Q3S3F6
cosubstrate NAD+, pH 8.0, 25C
12256
0.281
-
NAD+
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
14330
0.421
-
NAD+
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
14330
0.53
-
NAD+
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
14330
61.29
-
NADH
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
14331
90.61
-
NADH
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
14331
118.9
-
NADH
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
14331
0.18
-
NADP+
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
27497
0.268
-
NADP+
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
27497
2.07
-
NADP+
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
27497
101.4
-
NADPH
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
27498
296.2
-
NADPH
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
27498
331.2
-
NADPH
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
27498
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
160
240
L-threonine
-, O63067, O65027, Q3S3F6
pH 8.0, 25C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
10
Thermophilic bacterium
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
70
Thermophilic bacterium
-
no activity at 80C
PDB
SCOP
CATH
ORGANISM
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thiobacillus denitrificans (strain ATCC 25259)
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
strongly repressed by L-methionine; strongly repressed by L-threonine
-, D8WXQ1, D8WXQ2
strongly repressed by L-methionine; strongly repressed by L-threonine
-
-