Information on EC 1.1.1.3 - homoserine dehydrogenase:
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EC NUMBERCOMMENTARY
1.1.1.3-

RECOMMENDED NAMEGeneOntology No.
homoserine dehydrogenaseGO:0004412

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram		----
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram		bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activitiesArabidopsis thaliana-642340, 642341
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram		bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activitiesEscherichia coli-654640
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram		bifunctional enzyme showing aspartate kinase, 2.7.2.4, and homoserine dehydrogenase activitiesArabidopsis thaliana-657018
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
show the reaction diagram		ordered bi bi kinetic mechanism in which nicotinamide cofactor binds first and leaves last in the reaction sequenceGlycine maxO63067, O65027, Q3S3F6712490

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
homoserine biosynthesis-HOMOSERSYN-PWY

SYSTEMATIC NAMEIUBMB Comments
L-homoserine:NAD(P)+ oxidoreductaseThe 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).

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
AK-HDHEscherichia coli--654640
AK-HSD-1Glycine maxO63067, O65027, Q3S3F6; 712490
AK-HSDHArabidopsis thaliana--642340, 642341, 657018
AK-HSDHArabidopsis thaliana-isoform 1, bifunctional enzyme EC 2.7.2.4/EC 1.1.1.3662432
aspartate kinase-homoserine dehydrogenaseArabidopsis thaliana--642340, 642341, 657018
aspartate kinase-homoserine dehydrogenaseArabidopsis thaliana-bifunctional enzyme EC 2.7.2.4/EC 1.1.1.3662432
aspartokinase-homoserine dehydrogenase IEscherichia coli--654640
HDH----
hom-1Bacillus methanolicusD8WXQ1, D8WXQ2; 710978
homoserine dehydrogenase 1Lactobacillus plantarumQ88UF7, Q88Z09-670165
homoserine dehydrogenase 2Lactobacillus plantarumQ88UF7, Q88Z09-670165
HSD----
HSDH----
HSDHSaccharomyces cerevisiae--657018
HSDHChenopodium quinoa--689647

CAS REGISTRY NUMBERCOMMENTARY
9028-13-1-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thaliana-662432--Manually annotated by BRENDA team
Arabidopsis thalianabifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity642341--Manually annotated by BRENDA team
Arabidopsis thalianaslightly 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 activity642340O81852TREMBLManually annotated by BRENDA team
Arabidopsis thalianavar. Bensheim showing threonine and methionine prototrophy, bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity, gene akthr2657018--Manually annotated by BRENDA team
Bacillus methanolicusisoform hom-1710978D8WXQ1UniProtManually annotated by BRENDA team
Bacillus methanolicusisoform hom-2710978D8WXQ2UniProtManually annotated by BRENDA team
Chenopodium quinoatwo isozymes689647--Manually annotated by BRENDA team
Corynebacterium glutamicum-246394--Manually annotated by BRENDA team
Corynebacterium glutamicuma methionine-producing strain carrying mutations in the hom and the thrB genes688822--Manually annotated by BRENDA team
Escherichia coli-246387, 246390, 246398, 246400, 654640--Manually annotated by BRENDA team
Glycine max-712490Q3S3F6UniProtManually annotated by BRENDA team
Glycine maxbifunctional aspartokinase-homoserine dehydrogenase AK-HSD-1712490O65027UniProtManually annotated by BRENDA team
Glycine maxbifunctional aspartokinase-homoserine dehydrogenase AK-HSD-2712490O63067UniProtManually annotated by BRENDA team
Hordeum vulgarebarley246382--Manually annotated by BRENDA team
Lactobacillus plantarum-670165Q88UF7, Q88Z09SwissProtManually annotated by BRENDA team
Pisum sativumpea246382, 246388, 246391--Manually annotated by BRENDA team
Rhodospirillum rubrum-246389--Manually annotated by BRENDA team
Ricinus communiscastor bean246388--Manually annotated by BRENDA team
Saccharomyces cerevisiae-246396, 246402P31116UniprotManually annotated by BRENDA team
Saccharomyces cerevisiae-246397, 246399, 246401, 654955--Manually annotated by BRENDA team
Saccharomyces cerevisiaemutant strain M20-20D and wild-type strain S2207A657018--Manually annotated by BRENDA team
Serratia marcescensalso shows aspartase kinase activity246403--Manually annotated by BRENDA team
Spinacia oleraceaalso shows aspartase kinase activity; spinach246395--Manually annotated by BRENDA team
Streptomyces clavuligerusstrain NRRL 3585, gene hom688167Q56R01UniProtManually annotated by BRENDA team
Streptomyces clavuligerus NRRL 3585strain NRRL 3585, gene hom688167Q56R01UniProtManually annotated by BRENDA team
Thermophilic bacterium-246392--Manually annotated by BRENDA team
Thermus thermophilus-246393--Manually annotated by BRENDA team
Triticum aestivumwheat246388--Manually annotated by BRENDA team
Zea mayscorn246383, 246384, 246385, 246386--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionBacillus methanolicusD8WXQ1, D8WXQ2contrary 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 methanol710978

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Thermus thermophilus--246393-246393r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Escherichia coli--246387-246387r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Escherichia coli--246390-246390r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Escherichia coli--246398-246398r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiaeP31116-246396-246396-
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae--246402-246402-
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae--654955--?
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae--246401-246401r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Triticum aestivum--246388--r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Hordeum vulgare--246382-246382r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Spinacia oleracea--246395-246395r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Pisum sativum--246382-246382r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Pisum sativum--246388-246388r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Pisum sativum--246391-246391r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Serratia marcescens--246403-246403r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Ricinus communis--246388-246388r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Thermophilic bacterium--246392-246392r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Escherichia coli-kinetic mechanism246387--r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae-kinetic mechanism246401--r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Hordeum vulgare, Pisum sativum-third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine246382--r
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae-essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis654955--?
L-aspartate 4-semialdehyde + NADHL-homoserine + NAD+
show the reaction diagram		Glycine maxO63067, O65027, Q3S3F6-712490--r
L-aspartate 4-semialdehyde + NADPHL-homoserine + NADP+
show the reaction diagram		Escherichia coli--654640--r
L-aspartate 4-semialdehyde + NADPHL-homoserine + NADP+
show the reaction diagram		Arabidopsis thaliana--662432--?
L-aspartate 4-semialdehyde + NADPHL-homoserine + NADP+
show the reaction diagram		Glycine maxO63067, O65027, Q3S3F6-712490--r
L-aspartate 4-semialdehyde + NADPHL-homoserine + NADP+
show the reaction diagram		Escherichia coli-part of the aspartate pathway of amino acid biosynthesis654640--r
L-aspartate 4-semialdehyde + NADPH + H+L-homoserine + NADP+
show the reaction diagram		Lactobacillus plantarumQ88UF7, Q88Z09-670165--?
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Thermus thermophilus--246393--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Escherichia coli--246387-246387r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Escherichia coli--246390--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Saccharomyces cerevisiae--246401-246401r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Saccharomyces cerevisiae--246402-246402r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Triticum aestivum--246388--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Hordeum vulgare--246382--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Spinacia oleracea--246395--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Pisum sativum--246382, 246388, 246391--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Serratia marcescens--246403-246403r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Corynebacterium glutamicum--246394-246394-
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Ricinus communis--246388--r
L-homoserine + NAD(P)+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Thermophilic bacterium--246392-246392r
L-homoserine + NAD+L-aspartate 4-semialdehyde + NADH
show the reaction diagram		Glycine maxO63067, O65027, Q3S3F6-712490--r
L-homoserine + NADP+L-aspartate 4-semialdehyde + NADPH
show the reaction diagram		Saccharomyces cerevisiae, Arabidopsis thaliana--657018--?
L-homoserine + NADP+L-aspartate 4-semialdehyde + NADPH
show the reaction diagram		Arabidopsis thaliana--642341, 657018--r
L-homoserine + NADP+L-aspartate 4-semialdehyde + NADPH
show the reaction diagram		Arabidopsis thalianaO81852-642340--r
L-homoserine + NADP+L-aspartate 4-semialdehyde + NADPH
show the reaction diagram		Glycine maxO63067, O65027, Q3S3F6-712490--r
L-homoserine + NADP+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Streptomyces clavuligerusQ56R01-688167--r
additional information?-Glycine maxO63067, O65027, Q3S3F6enzyme does not show aspartate kinase activity712490---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Triticum aestivum, Pisum sativum, Ricinus communis--246388--
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Escherichia coli-kinetic mechanism246387--
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae-kinetic mechanism246401--
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Hordeum vulgare, Pisum sativum-third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine246382--
L-aspartate 4-semialdehyde + NAD(P)HL-homoserine + NAD(P)+
show the reaction diagram		Saccharomyces cerevisiae-essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis654955--
L-aspartate 4-semialdehyde + NADPHL-homoserine + NADP+
show the reaction diagram		Escherichia coli-part of the aspartate pathway of amino acid biosynthesis654640--
L-homoserine + NADP+L-aspartate 4-semialdehyde + NADPH
show the reaction diagram		Saccharomyces cerevisiae, Arabidopsis thaliana--657018--
L-homoserine + NADP+L-aspartate 4-semialdehyde + NAD(P)H
show the reaction diagram		Streptomyces clavuligerusQ56R01-688167--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
NAD+Thermophilic bacterium-low activity246392 2D-image
NADHHordeum vulgare, Pisum sativum--246382 2D-image
NADHPisum sativum, Ricinus communis, Triticum aestivum-threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only246388 2D-image
NADHSaccharomyces cerevisiae--246396, 654955 2D-image
NADHGlycine maxO63067, O65027, Q3S3F6GmHSD 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 cofactor712490 2D-image
NADP+Escherichia coli--246387 2D-image
NADP+Pisum sativum--246391 2D-image
NADP+Thermophilic bacterium-preferred246392 2D-image
NADP+Arabidopsis thaliana, Saccharomyces cerevisiae--657018 2D-image
NADP+Streptomyces clavuligerusQ56R01-688167 2D-image
NADPHHordeum vulgare, Pisum sativum-preferred246382 2D-image
NADPHZea mays--246385 2D-image
NADPHEscherichia coli--246387 2D-image
NADPHPisum sativum, Ricinus communis, Triticum aestivum-threonine sensitive isozyme can use NADPH or NADH, threonine insensitive isozyme can use NADPH only246388 2D-image
NADPHPisum sativum--246391 2D-image
NADPHSaccharomyces cerevisiae--246396, 654955 2D-image
NADPHArabidopsis thaliana--657018 2D-image
NADPHLactobacillus plantarumQ88UF7, Q88Z09; 670165 2D-image
NADPHStreptomyces clavuligerusQ56R01-688167 2D-image
NADPHGlycine maxO63067, O65027, Q3S3F6GmHSD 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 cofactor712490 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Cs+Pisum sativum, Ricinus communis, Triticum aestivum-activation of threonine sensitive enzyme246388
K+Pisum sativum, Ricinus communis, Triticum aestivum-activation of threonine sensitive isozyme246388
K+Thermophilic bacterium-required246392
K+Thermus thermophilus-activation246393
Li+Pisum sativum, Ricinus communis, Triticum aestivum-activation of threonine sensitive isozyme246388
Li+Thermophilic bacterium-can partially replace K+246392
Mg2+Arabidopsis thaliana-required for aspartate kinase activity642340, 642341, 657018
Na+Pisum sativum, Ricinus communis, Triticum aestivum-activation of threonine sensitive form246388
Na+Thermophilic bacterium-can partially replace K+246392
Na+Thermus thermophilus-activation246393
NH4+Pisum sativum, Ricinus communis, Triticum aestivum-activation of threonine sensitive isozyme246388
NH4+Thermophilic bacterium-can partially replace K+246392
Rb+Thermophilic bacterium-can partially replace K+246392

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(S)-2-amino-4-oxo-5-hydroxypentanoic acidSaccharomyces cerevisiae-RI-331246397, 246401 2D-image
2,2'-[thiobis[[2-(1,1-dimethylethyl)-5-methyl-4,1-phenylene]oxy]]bis-acetic acid diethyl esterSaccharomyces cerevisiae--654955 2D-image
4,4'-thiobis[2-(1,1-dimethylethyl)]-5-methyl-phenolSaccharomyces cerevisiae--654955 2D-image
4,4'-thiobis[2-(1,1-dimethylethyl)]-phenolSaccharomyces cerevisiae--654955 2D-image
4,4'-thiobis[2-(1-methylethyl)]-phenolSaccharomyces cerevisiae--654955 2D-image
4,4'-thiobis[5-methyl-2-(1-methylethyl)]-phenolSaccharomyces cerevisiae--654955 2D-image
4,4'-[1,2-ethanediylbis(thio)]bis[2,6-bis(1-methylpropyl)]-phenolSaccharomyces cerevisiae--654955 2D-image
4,4'-[1,2-ethanediylbis(thio)]bis[2-(1,1-dimethylethyl)-6-methyl]-phenolSaccharomyces cerevisiae--654955 2D-image
4-(1-methylheptyl)-1,3-benzenediolSaccharomyces cerevisiae--654955 2D-image
4-[[2-(2-furanyl)ethyl]thio]-phenolSaccharomyces cerevisiae--654955 2D-image
4-[[[4-(1,1-dimethylethyl)phenyl]thio]methyl]-2,6-bis(1-methylethyl)-phenolSaccharomyces cerevisiae--654955 2D-image
aspartateSpinacia oleracea--246395 2D-image
bis(4-chlorophenyl)ethyloxiranyl-silaneSaccharomyces cerevisiae--654955 2D-image
D-threonineThermophilic bacterium-slight246392 2D-image
DL-allo-threonineThermophilic bacterium--246392 2D-image
EGTASpinacia oleracea--246395 2D-image
H-(1,2,4-triazol-3-yl)-DL-alanineSaccharomyces cerevisiae--246401 2D-image
homoserineEscherichia coli--246400 2D-image
L-cysteineHordeum vulgare, Pisum sativum-slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme246382 2D-image
L-cysteinePisum sativum--246391 2D-image
L-cysteineThermophilic bacterium-slight246392 2D-image
L-cysteineCorynebacterium glutamicum--246394 2D-image
L-cysteineSpinacia oleracea--246395 2D-image
L-cysteineEscherichia coli--246398 2D-image
L-serineEscherichia coli--246398 2D-image
L-threonineHordeum vulgare, Pisum sativum--246382 2D-image
L-threonineZea mays--246384, 246385, 246386 2D-image
L-threonineEscherichia coli--246387, 246398 2D-image
L-threoninePisum sativum, Ricinus communis, Triticum aestivum-degree of inhibition depends on age of plant; sensitive and insensitive isozymes246388 2D-image
L-threoninePisum sativum-sensitive and insensitive isozymes246391 2D-image
L-threonineThermophilic bacterium--246392 2D-image
L-threonineThermus thermophilus-not inhibitory246393 2D-image
L-threonineCorynebacterium glutamicum--246394 2D-image
L-threonineSpinacia oleracea--246395 2D-image
L-threonineSaccharomyces cerevisiae--246399 2D-image
L-threonineSaccharomyces cerevisiae-weakly inhibits reverse but not forward reaction246401 2D-image
L-threonineSerratia marcescens--246403 2D-image
L-threonineArabidopsis thalianaO81852strong inhibition of both enzyme activities, aspartate dehydrogenase and aspartate kinase activity, by decreasing the affinity of the enzyme for substrate and cofactors, kinetic effects642340 2D-image
L-threonineArabidopsis thaliana-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 reactions642341 2D-image
L-threonineArabidopsis thaliana--657018 2D-image
L-threonineGlycine maxO63067, O65027, Q3S3F6-712490 2D-image
lysineSpinacia oleracea--246395 2D-image
methioninePisum sativum--246391 2D-image
methionineSpinacia oleracea--246395 2D-image
methionineSaccharomyces cerevisiae--246399 2D-image
NADP+Escherichia coli--246400 2D-image
p-chloromercuribenzoateRhodospirillum rubrum--246389 2D-image
ThrArabidopsis thaliana--662432 2D-image
ThrLactobacillus plantarumQ88UF7, Q88Z0990% inhibition of homoserine dehydrogenase 2 at 10 mM670165 2D-image
threonineCorynebacterium glutamicum-the methionine-producing strain contains a deregulated homoserine dehydrogenase that is not sensitive to feedback inhibition as the wild-type enzyme688822 2D-image
threonineChenopodium quinoa-feedback inhibition, one isozyme is resistant and another is sensitive to threonine inhibition, 46.9% inhibition at 1 mM, 63.9% at 5 mM689647 2D-image
TrifluoperazineSpinacia oleracea--246395 2D-image
TrisEscherichia coli--246390 2D-image
[2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid ethyl esterSaccharomyces cerevisiae--654955 2D-image
methionineSaccharomyces cerevisiae-weakly inhibits reverse but not forward reaction246401 2D-image
additional informationSaccharomyces cerevisiae-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 ester654955-
additional informationLactobacillus plantarumQ88UF7, Q88Z09Thr does not inhibit homoserine dehydrogenase 1670165-
additional informationChenopodium quinoa-Lys, Met, and S-2-aminoethyl-L-cysteine do not affect HSDH activity at 1-5 mM689647-
additional informationGlycine maxO63067, O65027, Q3S3F6enzyme is not inhibited by other aspartate-derived amino acids than threonine712490-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
CalmodulinSpinacia oleracea-in the presence of above 0.1 mM Ca2+246395 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.04-aspartate 4-semialdehydePisum sativum-isozyme II246382 2D-image
5.5-ATPArabidopsis thalianaO81852pH 8.0, 37°C, purified recombinant soluble enzyme642340 2D-image
0.1-DL-aspartate 4-semialdehydeSpinacia oleracea--246395 2D-image
11.6-L-aspartateArabidopsis thalianaO81852pH 8.0, 37°C, purified recombinant soluble enzyme642340 2D-image
0.066-L-aspartate 4-semialdehydePisum sativum-isozyme I246382 2D-image
0.08-L-aspartate 4-semialdehydePisum sativum-threonine insensitive isozyme246391 2D-image
0.098-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490 2D-image
0.1-L-aspartate 4-semialdehydeHordeum vulgare-isozyme I246382 2D-image
0.130.15L-aspartate 4-semialdehydeZea mays-threonine resistant isozyme246385 2D-image
0.130.15L-aspartate 4-semialdehydeTriticum aestivum-threonine resistant isozyme246388 2D-image
0.17-L-aspartate 4-semialdehydeEscherichia coli--246387 2D-image
0.240.25L-aspartate 4-semialdehydeZea mays-threonine sensitive isozyme246385 2D-image
0.240.25L-aspartate 4-semialdehydeTriticum aestivum-threonine sensitive isozyme246388 2D-image
0.360.4L-aspartate 4-semialdehydeHordeum vulgare-isozyme II246382 2D-image
0.5-L-aspartate 4-semialdehydePisum sativum-threonine sensitive isozyme246391 2D-image
0.5-L-aspartate 4-semialdehydeSpinacia oleracea--246395 2D-image
0.569-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490 2D-image
0.845-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490 2D-image
1.19-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490 2D-image
1.25-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490 2D-image
2.19-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490 2D-image
0.013-L-homoserineEscherichia coli--246387 2D-image
0.275-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C712490 2D-image
0.41-L-homoserineEscherichia coli-recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity654640 2D-image
0.68-L-homoserineEscherichia coli-recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity654640 2D-image
0.69-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C712490 2D-image
1.08-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C712490 2D-image
1.2-L-homoserineEscherichia coli-recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity654640 2D-image
5.2-L-homoserineArabidopsis thalianaO81852pH 8.0, 37°C, purified recombinant soluble enzyme642340 2D-image
9.57-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C712490 2D-image
13.4-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C712490 2D-image
17.2-L-homoserineEscherichia coli-recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity654640 2D-image
2.7-NAD+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
24.1-NAD+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
24.9-NAD+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.158-NADHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.19-NADHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.213-NADHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.3-NADHSpinacia oleracea--246395 2D-image
0.46-NADHPisum sativum-isozyme II246382 2D-image
0.034-NADP+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.073-NADP+Escherichia coli--246387 2D-image
0.166-NADP+Arabidopsis thalianaO81852pH 8.0, 37°C, purified recombinant soluble enzyme642340 2D-image
0.170.18NADP+Thermophilic bacterium--246392 2D-image
0.170.18NADP+Thermus thermophilus--246393 2D-image
0.235-NADP+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.245-NADP+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.027-NADPHPisum sativum-isozyme II246382 2D-image
0.028-NADPHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image
0.031-NADPHTriticum aestivum-threonine sensitive isozyme246388 2D-image
0.0320.036NADPHZea mays-threonine resistant isozyme246385 2D-image
0.0320.036NADPHTriticum aestivum-threonine resistant isozyme246388 2D-image
0.039-NADPHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C; pH 8.0, 25°C712490 2D-image
0.04-NADPHZea mays-threonine sensitive isozyme246385 2D-image
0.043-NADPHTriticum aestivum-threonine sensitive isozyme246388 2D-image
0.046-NADPHPisum sativum-isozyme I246382 2D-image
0.09-NADPHEscherichia coli--246387 2D-image
17.4-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C712490 2D-image
additional information-additional informationArabidopsis thalianaO81852kinetics642340-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.8-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490 2D-image
9.68-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490 2D-image
11.58-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490 2D-image
12.98-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490 2D-image
19.3-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490 2D-image
22.58-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490 2D-image
0.042-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C712490 2D-image
0.052-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C712490 2D-image
0.07-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C712490 2D-image
0.24-L-homoserineEscherichia coli-recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity654640 2D-image
0.51-L-homoserineEscherichia coli-recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity654640 2D-image
1.43-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C712490 2D-image
3.3-L-homoserineEscherichia coli-recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity654640 2D-image
7-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C712490 2D-image
10.15-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C712490 2D-image
24-L-homoserineEscherichia coli-recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity654640 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
5.29-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490222982
10.39-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490222982
16.22-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490222982
17.02-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490222982
26.73-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADH, pH 8.0, 25°C712490222982
28.54-L-aspartate 4-semialdehydeGlycine maxO63067, O65027, Q3S3F6cosubstrate NADPH, pH 8.0, 25°C712490222982
0.039-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C71249012256
0.082-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C71249012256
0.095-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C71249012256
0.256-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NADP+, pH 8.0, 25°C71249012256
0.731-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C71249012256
0.757-L-homoserineGlycine maxO63067, O65027, Q3S3F6cosubstrate NAD+, pH 8.0, 25°C71249012256
0.281-NAD+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249014330
0.421-NAD+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249014330
0.53-NAD+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249014330
61.29-NADHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249014331
90.61-NADHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249014331
118.9-NADHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249014331
0.18-NADP+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249027497
0.268-NADP+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249027497
2.07-NADP+Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249027497
101.4-NADPHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249027498
296.2-NADPHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249027498
331.2-NADPHGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C71249027498

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
160240L-threonineGlycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.00440.0046Chenopodium quinoa-enzyme activity at different seed developmental stages, overview689647
0.17-Triticum aestivum--246388
2.8-Pisum sativum--246388
5.4-Arabidopsis thalianaO81852purified recombinant soluble enzyme, forward reaction of aspartate kinase642340
6.8-Ricinus communis--246388
13-Glycine maxO63067, O65027, Q3S3F6pH 8.0, 25°C712490
18.87-Arabidopsis thalianaO81852purified recombinant soluble enzyme, reverse reaction of homoserine dehydrogenase642340
23.7-Saccharomyces cerevisiae--246402
51-Saccharomyces cerevisiae--246399
343-Zea mays--246385
360-Zea mays--246385
additional information-Corynebacterium glutamicum--246394

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7-Streptomyces clavuligerusQ56R01assay at688167
8-Arabidopsis thalianaO81852assay at642340
8-Arabidopsis thaliana-assay at642341
9-Thermus thermophilus--246393
9.8-Thermophilic bacterium--246392

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
810Thermophilic bacterium--246392

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Streptomyces clavuligerusQ56R01assay at room temperature688167
30-Corynebacterium glutamicum-assay at688822
37-Arabidopsis thalianaO81852assay at642340
37-Arabidopsis thaliana-assay at642341
70-Thermophilic bacterium--246392
additional information-Thermus thermophilus-above 50°C temperature dependent conformational change246393

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2070Thermophilic bacterium-no activity at 80°C246392

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
cell suspension cultureZea mays--246385Manually annotated by BRENDA team
leafHordeum vulgare, Pisum sativum--246382Manually annotated by BRENDA team
leafSpinacia oleracea--246395Manually annotated by BRENDA team
leafArabidopsis thaliana--657018Manually annotated by BRENDA team
seedChenopodium quinoa--689647Manually annotated by BRENDA team
seedlingZea mays--246383, 246384, 246386Manually annotated by BRENDA team
seedlingPisum sativum--246388, 246391Manually annotated by BRENDA team
seedlingRicinus communis, Triticum aestivum--246388Manually annotated by BRENDA team
stamenArabidopsis thaliana--657018Manually annotated by BRENDA team
meristemArabidopsis thaliana--657018Manually annotated by BRENDA team
additional informationArabidopsis thaliana-akthr2 is not or time-restricted expressed in stem, gynoecium, and during seed formation657018Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastHordeum vulgare, Pisum sativum-isozyme I9507246382Manually annotated by BRENDA team
cytoplasmHordeum vulgare, Pisum sativum-isozyme II5737246382Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1ebf, downloadSCOP (1ebf)CATH (1ebf)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1ebu, downloadSCOP (1ebu)CATH (1ebu)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1q7g, downloadSCOP (1q7g)CATH (1q7g)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1tve, downloadSCOP (1tve)CATH (1tve)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
2ejw, downloadSCOP (2ejw)CATH (2ejw)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
3mtj, downloadSCOP (3mtj)CATH (3mtj)Thiobacillus denitrificans (strain ATCC 25259)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
34000-Pisum sativum-gel filtration, isozyme II, cytoplasm246382
69000-Hordeum vulgare-gel filtration, isozyme II, cytoplasm246382
70000-Zea mays-gel filtration, threonine insensitive isozyme246385
70000-Glycine maxO63067, O65027, Q3S3F6gel filtration712490
75000-Pisum sativum, Triticum aestivum-gel filtration, threonine insensitive isozyme246388
80000-Ricinus communis-disc gel electrophoresis, threonine insensitive isozyme246388
81000-Saccharomyces cerevisiae-gel filtration246399
110000-Rhodospirillum rubrum-gel filtration, sedimentation equilibrium centrifugation246389
168000174000Hordeum vulgare, Pisum sativum-gel filtration, isozyme I, chloroplasts246382
190000-Zea mays-gel filtration threonine sensitive isozyme246385
220000-Rhodospirillum rubrum-gel filtration, aggregated form246389
220000-Spinacia oleracea-gel filtration246395
280000-Ricinus communis-disc gel electrophoresis, threonine sensitive isozyme246388
290000-Triticum aestivum-gel filtration, threonine sensitive isozyme246388
320000-Arabidopsis thalianaO81852in presence of L-threonine, gel filtration642340
320000-Arabidopsis thaliana-wild-type enzyme in presence of L-threonine, gel filtration642341
470000-Arabidopsis thalianaO81852in absence of L-threonine, gel filtration642340
470000-Arabidopsis thaliana-wild-type enzyme in absence of L-threonine, mutant enzymes Q443A and Q524A both in presence or absence of L-threonine, gel filtration642341

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Zea mays-x * 85000, SDS-PAGE, threonine sensitive isozyme246383
dimerZea mays-2 * 38000, SDS-PAGE, threonine resistant isozyme; x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme246385
dimerRhodospirillum rubrum-2 * 55000, SDS-PAGE246389
dimerSaccharomyces cerevisiae-crystal structure246396
dimerSaccharomyces cerevisiae-2 * 40000, SDS-PAGE246399
dimerGlycine maxO63067, O65027, Q3S3F62 * 40600, calculated, 2 * 40000, SDS-PAGE712490
tetramerZea mays-x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme246385
tetramerSpinacia oleracea-4 * 55000, SDS-PAGE246395
tetramerArabidopsis thalianaO81852in presence of L-threonine642340
hexamerArabidopsis thalianaO81852in absence of L-threonine642340
additional informationArabidopsis thaliana-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 495-534642341

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Saccharomyces cerevisiae-246396
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, modelingSaccharomyces cerevisiae-654955

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
70-Thermus thermophilus-up to246393
80-Thermus thermophilus-slow inactivation, protection by K+, Na+246393
90-Thermus thermophilus-rapid inactivation246393

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-80°C, purified recombinant soluble enzyme, at 3 mg/ml, stableArabidopsis thalianaO81852642340
-25°C, 50 mM potassium phosphate buffer, pH 7.2, 15% v/v glycerol, 1 mM EDTA, 1 mM threonine, 14 mM 2-mercaptoethanolPisum sativum-246391
-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 yearsZea mays-246384
-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 stableZea mays-246385

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinant enzymeArabidopsis thaliana-662432
native enzyme partially from seeds by ammonium sulfate fractionation and desalting gel filtrationChenopodium quinoa-689647
-Escherichia coli-246398
recombinant separated catalytic domainsEscherichia coli-654640
recombinant enzyme; recombinant enzyme; recombinant enzymeGlycine maxO63067, O65027, Q3S3F6712490
separation of the two isozymes using Matrex Gel Red A affinity chromatographyHordeum vulgare-246382
-Pisum sativum-246388, 246391
separation of the two isozymes using Blue-Sepharose chromatographyPisum sativum-246382
-Rhodospirillum rubrum-246389
-Ricinus communis-246388
-Saccharomyces cerevisiae-246399
overexpressed in Escherichia coliSaccharomyces cerevisiae-246402
-Spinacia oleracea-246395
-Thermophilic bacterium-246392
partialThermus thermophilus-246393
-Triticum aestivum-246388
-Zea mays-246383, 246384
threonine sensitive and threonine insensitive isozymesZea mays-246385

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
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 cellsArabidopsis thaliana-657018
overexpression of AK-HSDH isoform 1 in Escherichia coliArabidopsis thaliana-662432
introduction of the gene homFBR allele into strain HL1049Corynebacterium glutamicum-688822
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+Escherichia coli-654640
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coliGlycine maxO63067, O65027, Q3S3F6712490
expression in Escherichia coli; expression in Escherichia coliLactobacillus plantarumQ88UF7, Q88Z09670165
overexpression in Escherichia coliSaccharomyces cerevisiae-246402
gene hom, DNA and amino acid sequence determination and analysis, expression in the auxotroph mutant Escherichia coli CGSC 5075Streptomyces clavuligerusQ56R01688167

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
strongly repressed by L-methionine; strongly repressed by L-threonineBacillus methanolicusD8WXQ1, D8WXQ2710978

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Q443AArabidopsis thaliana-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, overview642341
additional informationArabidopsis thaliana-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 plants657018
Q524AArabidopsis thaliana-site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, overview642341
additional informationBacillus methanolicusD8WXQ1, D8WXQ2heterologous 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 methionine710978
G378ECorynebacterium glutamicum-feedback resistance of the enzyme246394
additional informationCorynebacterium glutamicum-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, overview688822
additional informationEscherichia coli-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 inhibition654640
H309ASaccharomyces cerevisiae-decrease of catalytic activity and elimination of substrate inhibition246402
additional informationSaccharomyces cerevisiae-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 cells657018
additional informationStreptomyces clavuligerusQ56R01construction 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, overview688167

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
denatures in 3 M guanidine-HCl and refolds by simple dilutionSaccharomyces cerevisiae-246399

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisBacillus methanolicusD8WXQ1, D8WXQ2contrary 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 methanol710978
pharmacologySaccharomyces cerevisiae-enzyme is a target for inhibitor design for construction of antimicrobial agents654955

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
246382Sainis, J.K.; Mayne, R.G.; Wallsgrove, R.M.; Lea, P.J.; Miflin, B.J.Localisation and characterisation of homoserine dehydrogenase isolated from barley and pea leavesPlanta152491-4961981Hordeum vulgare, Pisum sativum-
246383Krishnaswamy, S.; Bryan, J.K.Use of monoclonal antibodies for the purification and characterization of the threonine-sensitive isozyme of maize homoserine dehydrogenaseArch. Biochem. Biophys.246250-2621986Zea mays PubMed
246384Krishnaswamy, S.; Bryan, J.K.Ligand-induced interconversions of maize homoserine dehydrogenase among different statesArch. Biochem. Biophys.222449-4631983Zea mays PubMed
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246386Di Camelli, C.A.; Bryan, J.K.Comparison of sensitive and desensitized forms of maize homoserine dehydrogenasePlant Physiol.65176-1831980Zea mays PubMed
246387Wedler, F.C.; Ley, B.W.Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-IJ. Biol. Chem.2684880-48881993Escherichia coli PubMed
246388Grego, S.; Tricoli, D.; Di Marco, G.Comparison of homoserine dehydrogenase from different plant sourcesPhytochemistry191619-16231980Pisum sativum, Ricinus communis, Triticum aestivum-
246389Epstein, C.C.; Datta, P.Homoserine dehydrogenase of Rhodospirillum rubrum. Physical and chemical characterizationEur. J. Biochem.82453-4611978Rhodospirillum rubrum PubMed
246390Ogilvie, J.W.; Whitaker, S.C.Reaction of Tris with aldehydes. Effect of Tris on reactions catalyzed by homoserine dehydrogenase and glyceraldehyde-3-phosphate dehydrogenaseBiochim. Biophys. Acta445525-5361976Escherichia coli PubMed
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246392Cavari, B.Z.; Grossowicz, N.Properties of homoserine dehydrogenase in a thermophilic bacteriumBiochim. Biophys. Acta302183-1901973Thermophilic bacterium PubMed
246393Saiki, T.; Shinshi, H.; Arima, K.Studies on homoserine dehydrogenase from an extreme thermophile, Thermus flavus AT-62. Partial purification and propertiesJ. Biochem.741239-12481973Thermus thermophilus PubMed
246394Morbach, S.; Kelle, R.; Winkels, S.; Sahm, H.; Eggeling, L.Engineering the homoserine dehydrogenase and threonine dehydratase control points to analyse flux towards L-isoleucine in Corynebacterium glutamicumAppl. Microbiol. Biotechnol.45612-6201996Corynebacterium glutamicum-
246395Pavagi, S.; Kochhar, S.; Kochhar, V.K.; Sane, P.V.Purification and characterization of homoserine dehydrogenase from spinach leavesBiochem. Mol. Biol. Int.36649-6581995Spinacia oleracea PubMed
246396DeLaBarre, B.; Thompson, P.R.; Wright, G.D.; Berghuis, A.M.Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductasesNat. Struct. Biol.7238-2442000Saccharomyces cerevisiae PubMed
246397Yamaki, H.; Yamaguchi, M.; Imamura, H.; Suzuki, H.; Nishimura, T.; Saito, H.; Yamaguchi, H.The mechanism of antifungal action of (S)-2-amino-4-oxo-5-hydroxypentanoic acid, RI-331: The inhibition of homoserine dehydrogenase in Saccharomyces cerevisiaeBiochem. Biophys. Res. Commun.168837-8431990Saccharomyces cerevisiae PubMed
246398Hama, H.; Kayahara, T.; Tsuda, M.; Tsuchiya, T.Inhibition of homoserine dehydrogenase I by L-serine in Escherichia coliJ. Biochem.109604-6081991Escherichia coli PubMed
246399Yumoto, N.; Kawata, Y.; Noda, S.; Tokushige, M.Rapid purification and characterization of homoserine dehydrogenase from Saccharomyces cerevisiaeArch. Biochem. Biophys.285270-2751991Saccharomyces cerevisiae PubMed
246400Angeles, T.S.; Viola, R.E.The kinetic mechanism of the bifunctional enzyme aspartokinase - Homoserine dehydrogenase I from Escherichia coliArch. Biochem. Biophys.28396-1011990Escherichia coli PubMed
246401Jacques, S.L.; Ejim, L.J.; Wright, G.D.Homoserine dehydrogenase from Saccharomyces cerevisiae: kinetic mechanism and stereochemistry of hydride transferBiochim. Biophys. Acta154442-542001Saccharomyces cerevisiae PubMed
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246403Omori, K.; Komatsubara, S.Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I analyzed by using site-directed mutagenesisJ. Bacteriol.175959-9651993Serratia marcescens PubMed
642340Paris, S.; Wessel, P.M.; Dumas, R.Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thalianaProtein Expr. Purif.24105-1102002Arabidopsis thaliana PubMed
642341Paris, S.; Viemon, C.; Curien, G.; Dumas, R.Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonineJ. Biol. Chem.2785361-53662003Arabidopsis thaliana PubMed
654640James, C.L.; Viola, R.E.Production and characterization of bifunctional enzymes. Domain swapping to produce new bifunctional enzymes in the aspartate pathwayBiochemistry413720-37252002Escherichia coli PubMed
654955Ejim, L.; Mirza, I.A.; Capone, C.; Nazi, I.; Jenkins, S.; Chee, G.L.; Berghuis, A.M.; Wright, G.D.New phenolic inhibitors of yeast homoserine dehydrogenaseBioorg. Med. Chem.123825-38302004Saccharomyces cerevisiae PubMed
657018Rognes, S.E.; Dewaele, E.; Aas, S.F.; Jacobs, M.; Frankard, V.Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutantPlant Mol. Biol.51281-2942003Arabidopsis thaliana, Saccharomyces cerevisiae PubMed
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670165Cahyanto, M.N.; Kawasaki, H.; Nagashio, M.; Fujiyama, K.; Seki, T.Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarumMicrobiology152105-1122006Lactobacillus plantarum PubMed
688167Yilmaz, E.I.; Caydasi, A.K.; Ozcengiz, G.Targeted disruption of homoserine dehydrogenase gene and its effect on cephamycin C production in Streptomyces clavuligerusJ. Ind. Microbiol. Biotechnol.351-72008Streptomyces clavuligerus PubMed
688822Park, S.D.; Lee, J.Y.; Sim, S.Y.; Kim, Y.; Lee, H.S.Characteristics of methionine production by an engineered Corynebacterium glutamicum strainMetab. Eng.9327-3362007Corynebacterium glutamicum PubMed
689647Varisi, V.A.; Camargos, L.S.; Aguiar, L.F.; Christofoleti, R.M.; Medici, L.O.; Azevedo, R.A.Lysine biosynthesis and nitrogen metabolism in quinoa (Chenopodium quinoa): study of enzymes and nitrogen-containing compoundsPlant Physiol. Biochem.4611-182008Chenopodium quinoa PubMed
710978Brautaset, T.; Jakobsen, O.M.; Degnes, K.F.; Netzer, R.; Naerdal, I.; Krog, A.; Dillingham, R.; Flickinger, M.C.; Ellingsen, T.E.Bacillus methanolicus pyruvate carboxylase and homoserine dehydrogenase I and II and their roles for L-lysine production from methanol at 50 degrees CAppl. Microbiol. Biotechnol.87951-9642010Bacillus methanolicus PubMed
712490Schroeder, A.C.; Zhu, C.; Yanamadala, S.R.; Cahoon, R.E.; Arkus, K.A.; Wachsstock, L.; Bleeke, J.; Krishnan, H.B.; Jez, J.M.Threonine-insensitive homoserine dehydrogenase from soybean: genomic organization, kinetic mechanism, and in vivo activityJ. Biol. Chem.285827-8342010Glycine max PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.3)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)