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Literature summary for 1.1.1.3 extracted from

  • Tomonaga, Y.; Kaneko, R.; Goto, M.; Ohshima, T.; Yoshimune, K.
    Structural insight into activation of homoserine dehydrogenase from the archaeon (2015), Biochem. Biophys. Rep., 3, 14-17.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
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 Sulfurisphaera tokodaii

Cloned(Commentary)

Cloned (Comment) Organism
gene hom, recombinant overexpression in Escherichia coli strain BL21(DE3) Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.21
-
L-homoserine pH 8.0, 30°C, oxidized enzyme Sulfurisphaera tokodaii
0.31
-
NAD+ pH 8.0, 30°C, oxidized enzyme Sulfurisphaera tokodaii
0.33
-
NAD+ pH 8.0, 30°C, reduced enzyme Sulfurisphaera tokodaii
0.54
-
L-homoserine pH 8.0, 30°C, reduced enzyme Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-homoserine + NAD(P)+ Sulfurisphaera tokodaii
-
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
r
L-homoserine + NAD(P)+ Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
r

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii F9VNG5
-
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 F9VNG5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 70°C for 3 h, anion exchange chromatography, dialysis, and ultrafiltration Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-homoserine + NAD(P)+
-
Sulfurisphaera tokodaii L-aspartate 4-semialdehyde + NAD(P)H + H+
-
r
L-homoserine + NAD(P)+
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 L-aspartate 4-semialdehyde + NAD(P)H + H+
-
r
L-homoserine + NAD+
-
Sulfurisphaera tokodaii L-aspartate 4-semialdehyde + NADH + H+
-
r
L-homoserine + NAD+
-
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 L-aspartate 4-semialdehyde + NADH + H+
-
r

Subunits

Subunits Comment Organism
homodimer dimeric enzyme structure, overview Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
HSD
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Sulfurisphaera tokodaii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Sulfurisphaera tokodaii
NADH
-
Sulfurisphaera tokodaii
NADP+
-
Sulfurisphaera tokodaii
NADPH
-
Sulfurisphaera tokodaii

General Information

General Information Comment Organism
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 Sulfurisphaera tokodaii