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 (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 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 | Comment | Organism | Structure |
---|---|---|---|
NaCl | activates, best at 0.4 M | Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
221000 | - |
recombinant His-tagged enzyme, gel filtration | Bacillus subtilis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P19582 | - |
- |
Bacillus subtilis 168 | P19582 | - |
- |
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 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 | 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 | 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 | Comment | Organism |
---|---|---|
BsHSD | - |
Bacillus subtilis |
hom | - |
Bacillus subtilis |
HSD | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | 40 | - |
Bacillus subtilis |
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 Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
54.8 | - |
melting temperature of recombinant enzyme BsHSD | Bacillus subtilis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
L-HSE oxidation in the presence of 0.4 M NaCl | Bacillus subtilis |
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 | Comment | Organism | Structure |
---|---|---|---|
NADP+ | enzyme BsHSD exclusively prefers NADP+ to NAD+ | Bacillus subtilis | |
NADPH | - |
Bacillus subtilis |
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 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 |