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Literature summary for 1.1.1.3 extracted from
- Molecular and enzymatic features of homoserine dehydrogenase from Bacillus subtilis (2020), J. Microbiol. Biotechnol., 30, 1905-1911 .
Application
| Application | Comment | Organism |
|---|---|---|
| agriculture | enzyme HSD is used in the development of pesticides | Bacillus subtilis |
| synthesis | enzyme HSD is utilized in the large scale production of L-lysine | Bacillus subtilis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene hom, recombinant overexpression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), expression of soluble enzyme at lower temperature of 25°C | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation, Michaelis-Menten kinetics, overview | Bacillus subtilis | |
| 0.039 | - |
NADP+ | pH 9.0, 25°C, recombinant enzyme | Bacillus subtilis |  |
| 35.08 | - |
L-homoserine | pH 9.0, 25°C, recombinant enzyme | Bacillus subtilis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | activates, best at 0.4 M | Bacillus subtilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 221000 | - |
recombinant His-tagged enzyme, gel filtration | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-homoserine + NADP+ | Bacillus subtilis | - |
L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
| L-homoserine + NADP+ | Bacillus subtilis 168 | - |
L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P19582 | - |
- |
| Bacillus subtilis 168 | P19582 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) to homogeneity by nickel affinity chromatography and two different steps of gel filtration | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.48 | 2.01 | purified recombinant enzyme expressed in Escherichia coli, pH 9.0, 25°C | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-homoserine + NADP+ | - |
Bacillus subtilis | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
| L-homoserine + NADP+ | the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation | Bacillus subtilis | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
| L-homoserine + NADP+ | - |
Bacillus subtilis 168 | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
| L-homoserine + NADP+ | the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation | Bacillus subtilis 168 | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
| additional information | enzyme BsHSD exclusively prefers NADP+ to NAD+ | Bacillus subtilis | ? | - |
- |
|
| additional information | enzyme BsHSD exclusively prefers NADP+ to NAD+ | Bacillus subtilis 168 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs | Bacillus subtilis |
| tetramer | 4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BsHSD | - |
Bacillus subtilis |
| hom | - |
Bacillus subtilis |
| HSD | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 40 | - |
Bacillus subtilis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 50 | 45% of maximal activity at 25°C and 50°C, maximal activity at 35-40°C, 75% at 45°C, 65% at 35°C, profile overview | Bacillus subtilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 54.8 | - |
melting temperature of recombinant enzyme BsHSD | Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.07 | - |
L-homoserine | pH 9.0, 25°C, recombinant enzyme | Bacillus subtilis | |
| 1.1 | - |
NADP+ | pH 9.0, 25°C, recombinant enzyme | Bacillus subtilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
L-HSE oxidation in the presence of 0.4 M NaCl | Bacillus subtilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9.5 | BsHSD is maximally active in L-HSE oxidation at pH 9.0 and is the least active at pH 7.0 with only 1.1% of the maximal activity | Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | enzyme BsHSD exclusively prefers NADP+ to NAD+ | Bacillus subtilis | |
| NADPH | - |
Bacillus subtilis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine | Bacillus subtilis |
| additional information | three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview | Bacillus subtilis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.031 | - |
L-homoserine | pH 9.0, 25°C, recombinant enzyme | Bacillus subtilis | |
| 28.2 | - |
NADP+ | pH 9.0, 25°C, recombinant enzyme | Bacillus subtilis | |
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