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Enzyme Nomenclature
Information on EC 1.1.1.3 - homoserine dehydrogenase
for references in articles please use BRENDA:EC1.1.1.3
Word Map on EC 1.1.1.3
- 1.1.1.3
- l-threonine
-
threonine-sensitive
- corynebacterium
- glutamicum
- l-lysine
- semialdehyde
- dihydrodipicolinate
- brevibacterium
- l-isoleucine
-
2.7.2.4
-
aspartate-derived
-
i-homoserine
-
rhodospirillum
- lactofermentum
-
lysine-sensitive
-
feedback-insensitive
- flavum
-
feedback-resistant
- pharmacology
- synthesis
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.3
-
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RECOMMENDED NAME
GeneOntology No.
homoserine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities
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L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities
-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, 2.7.2.4, and homoserine dehydrogenase activities
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L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
ordered bi bi kinetic mechanism in which nicotinamide cofactor binds first and leaves last in the reaction sequence
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview
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L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9028-13-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity
-
-
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
var. Bensheim showing threonine and methionine prototrophy, bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity, gene akthr2
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a methionine-producing strain carrying mutations in the hom and the thrB genes
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
evolution
-
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
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malfunction
HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes
malfunction
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HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes
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metabolism
-
homoserine dehydrogenase is a key enzyme in the L-threonine pathway
metabolism
-
homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
metabolism
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homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine
metabolism
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
metabolism
-
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
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metabolism
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homoserine dehydrogenase is a key enzyme in the L-threonine pathway
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metabolism
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homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine; homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine
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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
physiological function
-
the enzyme is naturally allosterically regulated by threonine and isoleucine
physiological function
-
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
physiological function
-
the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway
physiological function
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
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
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physiological function
-
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine; the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway
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physiological function
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homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
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additional information
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structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
additional information
structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207
additional information
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structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207
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additional information
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structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
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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
L-aspartate 4-semialdehyde + NADH
L-homoserine + NAD+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
-
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
Thermophilic bacterium
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-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
part of the aspartate pathway of amino acid biosynthesis
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
-
-
r
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
-
?
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
-
?
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
Thermophilic bacterium
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-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
-
r
additional information
?
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enzyme does not show aspartate kinase activity
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-
-
additional information
?
-
enzyme does not show aspartate kinase activity
-
-
-
additional information
?
-
enzyme does not show aspartate kinase activity
-
-
-
additional information
?
-
enzyme does not show aspartate kinase activity
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
part of the aspartate pathway of amino acid biosynthesis
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis
-
-
?
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
Q56R01
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
Q56R01
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
F9VNG5
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
F9VNG5
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
O58802
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
O58802
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
Q5AIA2
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
P08499
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
P08499
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
P46806
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
P46806
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
A0A0H2WVX4
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
A0A0H2WVX4
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NADP does not act as a cofactor for this enzyme, but as a strong inhibitor of NAD+-dependent oxidation of Hse, analysis of the cofactor-binding site of the enzyme, Pyrococcus horikoshii HseDH shows a unique cofactor binding mode, which is not observed in conventional NAD(P)-dependent dehydrogenases. Superposition of the Hse/NADPH-bound K57A structure onto the NADPH-bound wild-type structure shows that the NADPH molecule in the mutant structure is positioned/configured nearly identically to the NADPH molecule in the wild-type structure, except for the positioning of the C2 phosphate group of the adenine ribose. The C2 phosphate is tightly held in position through five surrounding hydrogen bonds in the wild-type enzyme. In K57A mutant the C2 phosphate group is rotates in a clockwise direction around C2B of NADPH by about 30° relative to the wild-type structure. The guanidino group of Arg40 in the mutant is also rotated clockwise by about 90° around the NE atom of Arg40 relative to the wild-type structure
-
NADH
-
threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only
NADH
-
threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only
NADH
-
threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only
NADH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
NADP+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
NADPH
-
threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only
NADPH
-
threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only
NADPH
-
threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only
NADPH
GmHSD displays a 1.6fold preference for NADPH over NADH as the cofactor in the oxidation reaction. In the reduction reaction NADP+ is favored nearly 4fold as the cofactor
NADPH
no activity of the wild-type enzyme with NADPH, but only with enzyme mutants R40A and K57A
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cs+
K+
Li+
Na+
NH4+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene
-
2,2'-[thiobis[[2-(1,1-dimethylethyl)-5-methyl-4,1-phenylene]oxy]]bis-acetic acid diethyl ester
-
-
4,4'-[1,2-ethanediylbis(thio)]bis[2,6-bis(1-methylpropyl)]-phenol
-
-
-
4,4'-[1,2-ethanediylbis(thio)]bis[2-(1,1-dimethylethyl)-6-methyl]-phenol
-
-
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
competitive to L-aspartate 4-semialdehyde, enzyme binding structure anaysis from crystal structure, overview
-
4-[[[4-(1,1-dimethylethyl)phenyl]thio]methyl]-2,6-bis(1-methylethyl)-phenol
-
-
L-lysine
-
allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine
[2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid ethyl ester
-
-
L-cysteine
-
slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme
L-cysteine
-
slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme
L-threonine
strong inhibition of both enzyme activities, aspartate dehydrogenase and aspartate kinase activity, by decreasing the affinity of the enzyme for substrate and cofactors, kinetic effects
L-threonine
-
the regulatory domain of the enzyme contains 2 binding sites, interaction with Gln443 leads to inhibition of the aspartate kinase activity and facilitates the binding of a second threonine on Gln524 leading to inhibition of the homoserine dehydrogenase activity, inhibition of the forward reactions
L-threonine
-
the enzyme activity is subjected to feedback regulation by L-threonine
L-threonine
-
the natural threonine binding sites of the enzyme are predicted and verified by mutagenesis experiments
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
NADP+
NADP+ does not act as a cofactor for this enzyme, but as a strong inhibitor of NAD+-dependent oxidation of Hse, evaluation of the factors responsible for the NADP+-mediated inhibition
threonine
-
feedback inhibition, one isozyme is resistant and another is sensitive to threonine inhibition, 46.9% inhibition at 1 mM, 63.9% at 5 mM
threonine
-
the methionine-producing strain contains a deregulated homoserine dehydrogenase that is not sensitive to feedback inhibition as the wild-type enzyme
additional information
-
Lys, Met, and S-2-aminoethyl-L-cysteine do not affect HSDH activity at 1-5 mM
-
additional information
-
the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
-
additional information
-
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
-
Thr does not inhibit homoserine dehydrogenase 1
-
additional information
-
no inhibition by [2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid and 4-amino-butyric acid 2-tert-butyl-4-(3-tert-butyl-4-hydroxy-phenylsulfanyl)-phenyl ester
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
the enzyme is 2.5fold activated by the addition of 0.8 mM dithiothreitol. The activation is caused by cleavage of the disulfide bond formed between two cysteine residues in the C-terminal regions of the two subunits
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.6
L-aspartate
pH 8.0, 37°C, purified recombinant soluble enzyme
0.098
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
0.569
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
0.845
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
1.19
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
1.25
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
2.19
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
0.41
L-homoserine
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity
0.68
L-homoserine
-
recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity
1.2
L-homoserine
-
recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity
5.2
L-homoserine
pH 8.0, 37°C, purified recombinant soluble enzyme
17.2
L-homoserine
-
recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity
additional information
additional information
enzyme HseDH shows typical Michaelis-Menten kinetics for oxidation
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.8
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
9.68
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
11.58
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
12.98
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
19.3
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
22.58
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
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
3.3
L-homoserine
-
recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity
24
L-homoserine
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.29
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
10.39
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
16.22
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
17.02
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
26.73
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
28.54
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0131
(2S)-2-[[4-(propan-2-yl)phenyl]sulfanyl]propanenitrile
pH and temperature not specified in the publication
0.01307
1-tert-butyl-4-[(difluoromethyl)sulfanyl]benzene
pH and temperature not specified in the publication
0.00963
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene
pH and temperature not specified in the publication
0.01568
3-[(4-tert-butylphenyl)sulfanyl]propane-1-thiol
pH and temperature not specified in the publication
0.01
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
pH and temperature not specified in the publication
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0051
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
Mycobacterium leprae
P46806
pH and temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0044 - 0.0046
-
enzyme activity at different seed developmental stages, overview
5.4
purified recombinant soluble enzyme, forward reaction of aspartate kinase
18.87
purified recombinant soluble enzyme, reverse reaction of homoserine dehydrogenase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
-
the catalytic activity of the enzyme for the conversion of L-homoserine to L-aspartate 4-semialdehyde (the reverse reaction) is enhanced at basic pH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
additional information
-
above 50°C temperature dependent conformational change
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
akthr2 is not or time-restricted expressed in stem, gynoecium, and during seed formation
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thiobacillus denitrificans (strain ATCC 25259)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
55000
70000
75000
168000 - 174000
220000
320000
470000
470000
-
wild-type enzyme in absence of L-threonine, mutant enzymes Q443A and Q524A both in presence or absence of L-threonine, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
dimer
-
2 * 38000, SDS-PAGE, threonine resistant isozyme; x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
homodimer
-
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
-
homodimer
-
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
homodimer
-
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
-
additional information
-
primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534
additional information
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
additional information
-
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
-
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for the purified ligand-free recombinant wild-type enzyme: sitting drop vapor diffusion method, mixing of 0.001 ml of 12.0 mg/ml protein solution with an equal volume of mother liquor composed of 0.1 M potassium phosphate, pH 6.2, and 20% MPD, 2 days, 20°C, for the homoserine-bound K57A mutant enzyme: sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution containing 1 mM homoserine with 0.002 ml of mother liquor containing 16% polyethylene glycol monomethyl ether 2000 and 0.1 M citrate buffer, pH 6.5, 7 days, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling
10 mg/ml purified recombinant enzyme, in TAPS, pH 8.5, in complex with inhibitor 4,4'-thiobis[2-(1-methylethyl)-phenol] in a molar ratio of 1:1, precipitant solution contains either 0.1 CHES, pH 9.5, 35% PEG 600 or 0.1 M CHES, pH 8.5, 40% PEG 400, and 0.2 M NaCl, 0.005 ml protein complex solution are equilibrated against 0.7 ml of precipitant solution using sitting drop technique, 3 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling
-
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, hanging drop and sitting drop methods of vapour diffusion, 8 mg/ml protein solution is mixed with reservoir solution, different conditions involving addition of 0.2 M magnesium acetate and PEG 3350 or 8000, and 3.5% glycerol, overview. X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
-
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
-
purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12°C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 12
purified recombinant His-tagged enzyme, 10 min, 50°C, stable at
741408
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
half-life of mutant L200F/D215K is 4.16 h, of mutant L200F 3.71 h
75
purified recombinant His-tagged enzyme, 10 min, retains full activity
90
90
purified recombinant His-tagged enzyme, 10 min, retains 70% activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
additional information
-
both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 M potassium phosphate buffer, pH 7.5, 1.0 mM EDTA, 2.0 mM dithioerythritol, 5.0 mM L-threonine, 20% v/v glycerol, at least 2 years
-
-20°C, 30 mM potassium phosphate buffer, pH 7.5, 50% v/v glycerol, threonine resistant isozyme at least 2 months stable, threonine sensitive isozyme at least 4 months stable
-
-25°C, 50 mM potassium phosphate buffer, pH 7.2, 15% v/v glycerol, 1 mM EDTA, 1 mM threonine, 14 mM 2-mercaptoethanol
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially from seeds by ammonium sulfate fractionation and desalting gel filtration
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 70°C for 3 h, anion exchange chromatography, dialysis, and ultrafiltration
recombinant His-tagged enzyme from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) codon plus-RIPL by heat treatment at 90°C for 10 min, nickel affinity chromatography, dialysis, gel filtration, and ultrafiltration
separation of the two isozymes using Matrex Gel Red A affinity chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both catalytic domains of the enzyme, performing each one of the enzyme activities, are expressed separately with or without the interface region, resulting in increased activity of each domain compared to the wild-type bifunctional holoenzyme, the isolated catalytic domains are no longer allosterically regulated, expression of hybrid holoenzyme AKIII-HDHI+
-
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
gene akthr2, DNA sequence determination and analysis, located on chromosome 4, subcloning in Escherichia coli strain DH5alpha, functional complementation of the Saccharomyces cerevisiae homoserine dehydrogenase-deficient hom6 mutant strain and of the aspartate kinase-deficient hom3 mutant strain, conferring L-threonine and L-methionine prototrophy to the yeast cells
-
gene hom, DNA and amino acid sequence determination and analysis, expression in the auxotroph mutant Escherichia coli CGSC 5075
gene hom, recombinant expression of His-tagged enzyme in Echerichia coli strain Rosetta (DE3) pLysS
-
gene hom, recombinant expression of His-tagged wild-type and mutant enzymes in Echerichia coli strain Rosetta (DE3) pLysS
-
gene hom, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene hom1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), recombinant overexpression of constructs comprising the enzyme with homoserine kinase, aspartate kinase, acetohydroxy acid synthase, or threonine dehydratase, overview
-
gene HOM6, DNA and amino acid sequence determination and analysis from the strain SC5314 genome, sequence comparison, reintegration of the gene encoding the wild-type enzyme into HOM6-deletion strains
gene PH1075, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) codon plus-RIPL
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
strongly repressed by L-methionine; strongly repressed by L-threonine
strongly repressed by L-methionine; strongly repressed by L-threonine
strongly repressed by L-methionine; strongly repressed by L-threonine
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q443A
-
site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, asparate kinase activity is completely insensitive to inhibition by L-threonine, overview
Q524A
-
site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, overview
G378S
L200F
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F/D215K
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
L200F
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 degree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
-
L200F/D215K
-
site-directed mutagenesis, compared to mutant L200F, the double mutant shows 2 dgree higher optimum temperature, 1.24 times higher activity, but the same pH optimum of pH 7.5 as mutant L200F. Both mutants L200F/D215K and L200F show good resistance to organic solvents and metal ions
-
K57Aa
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme
R40A
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is decreased compared to the wild-type enzyme
K57Aa
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme
-
R40A
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is decreased compared to the wild-type enzyme
-
H309A
-
decrease of catalytic activity and elimination of substrate inhibition
additional information
G378S
-
construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview
G378S
-
construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview
-
additional information
-
construction of transgenic Arabidopsis thaliana plants by transformation with gene akthr2 via Agrobacterium tumefaciens infection, determination of expression patterns of the gene akthr1 ans akthr2 in the transgenic plants
additional information
-
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine; heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine; heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine; heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
additional information
-
heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine; heterologous expression in a hom-negative Escherichia coli mutant Gif 102, not able to grow on minimal medium unless added 1.5 mM of both L-threonine and L-methionine results in strains growing well on minimal agar plates without added threonine and methionine
-
additional information
-
generation of HOM6-deleted (HOM6/hom6DELT and hom6DELTA/hom6DELTA) and HOM6-reintegrated (hom6DELTA/hom6DELTA::HOM6 and hom6DELTA::HOM6/hom6DELTA::HOM6) strains
additional information
generation of HOM6-deleted (HOM6/hom6DELT and hom6DELTA/hom6DELTA) and HOM6-reintegrated (hom6DELTA/hom6DELTA::HOM6 and hom6DELTA::HOM6/hom6DELTA::HOM6) strains
additional information
-
generation of HOM6-deleted (HOM6/hom6DELT and hom6DELTA/hom6DELTA) and HOM6-reintegrated (hom6DELTA/hom6DELTA::HOM6 and hom6DELTA::HOM6/hom6DELTA::HOM6) strains
-
additional information
-
engineering of a Corynebacterium glutamicum strain HL1049 for effective production of methionine by elimination of the threonine synthesis gene and desensitizing the homoserine dehydrogenase versus inhibition by threonine, analysis of the amino acid spectrum of the engineered strain, overview
additional information
-
releasing the enzymes of the L-threonine biosynthesis pathway from feedback control and coordinating their expression plays a pivotal role in engineering Corynebacterium glutamicum into L-isoleucine producers, construction of transgenic Corynebacterium glutamicum with deregulated L-threonine biosynthesis pathway enzymes for enhanced L-isoleucine biosynthesis
additional information
-
design of an artificial allosteric enzyme to sense an unnatural signal for a precise and dynamical control of fluxes of growth-essential but byproduct pathways in metabolic engineering of industrial microorganisms. The natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
additional information
-
releasing the enzymes of the L-threonine biosynthesis pathway from feedback control and coordinating their expression plays a pivotal role in engineering Corynebacterium glutamicum into L-isoleucine producers, construction of transgenic Corynebacterium glutamicum with deregulated L-threonine biosynthesis pathway enzymes for enhanced L-isoleucine biosynthesis
-
additional information
-
construction of a hybrid enzyme AKIII-HDHI+ by fusing a wild-type monofunctional aspartate kinase AKIII enzyme to the thrA2+ gene, encoding the homoserine dehydrogenase including the interface region of the wild-type bifunctional enzyme, the hybrid enzyme shows highly improved kinetic properties for homoserine dehydrogenase activity, and is not sensitive to L-threonine inhibition
additional information
-
mutant strain M20-20D is deficient in gene HOM6 and shows no activity, the defect can be complemented by recombinant expression of the Arabidopsis thaliana gene akthr2 in the mutant yeast cells
additional information
construction of a hom disruption mutant by insertional inactivation via double crossover leading to up to 4.3fold and 2fold increases in intracellular free L-lysine concentration and specific cephamycin C production, respectively, during stationary phase in chemically defined medium, overview
additional information
-
construction of a hom disruption mutant by insertional inactivation via double crossover leading to up to 4.3fold and 2fold increases in intracellular free L-lysine concentration and specific cephamycin C production, respectively, during stationary phase in chemically defined medium, overview
-
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
pharmacology
-
enzyme is a target for inhibitor design for construction of antimicrobial agents
synthesis
additional information
drug development
the enzyme might be a good target for anti-fungal drug development
drug development
-
the enzyme might be a good target for anti-fungal drug development
-
synthesis
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
synthesis
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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
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additional information
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HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices
additional information
HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices
additional information
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HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices
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