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 (Comment) | Organism |
---|---|
gene hom, recombinant overexpression in Escherichia coli strain BL21(DE3) | Sulfurisphaera tokodaii |
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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Sulfurisphaera tokodaii | F9VNG5 | - |
- |
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 | F9VNG5 | - |
- |
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 | 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 | Comment | Organism |
---|---|---|
homodimer | dimeric enzyme structure, overview | Sulfurisphaera tokodaii |
Synonyms | Comment | Organism |
---|---|---|
HSD | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Sulfurisphaera tokodaii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Sulfurisphaera tokodaii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Sulfurisphaera tokodaii | |
NADH | - |
Sulfurisphaera tokodaii | |
NADP+ | - |
Sulfurisphaera tokodaii | |
NADPH | - |
Sulfurisphaera tokodaii |
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 |