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Literature summary extracted from

  • Kim, D.H.; Nguyen, Q.T.; Ko, G.S.; Yang, J.K.
    Molecular and enzymatic features of homoserine dehydrogenase from Bacillus subtilis (2020), J. Microbiol. Biotechnol., 30, 1905-1911 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.3 agriculture enzyme HSD is used in the development of pesticides Bacillus subtilis
1.1.1.3 synthesis enzyme HSD is utilized in the large scale production of L-lysine Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.3 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.3 additional information
-
additional information the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation, Michaelis-Menten kinetics, overview Bacillus subtilis
1.1.1.3 0.039
-
NADP+ pH 9.0, 25°C, recombinant enzyme Bacillus subtilis
1.1.1.3 35.08
-
L-homoserine pH 9.0, 25°C, recombinant enzyme Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.3 NaCl activates, best at 0.4 M Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.3 221000
-
recombinant His-tagged enzyme, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.3 L-homoserine + NADP+ Bacillus subtilis
-
L-aspartate 4-semialdehyde + NADPH + H+
-
r
1.1.1.3 L-homoserine + NADP+ Bacillus subtilis 168
-
L-aspartate 4-semialdehyde + NADPH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.3 Bacillus subtilis P19582
-
-
1.1.1.3 Bacillus subtilis 168 P19582
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.3 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.3 1.48 2.01 purified recombinant enzyme expressed in Escherichia coli, pH 9.0, 25°C Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.3 L-homoserine + NADP+
-
Bacillus subtilis L-aspartate 4-semialdehyde + NADPH + H+
-
r
1.1.1.3 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
1.1.1.3 L-homoserine + NADP+
-
Bacillus subtilis 168 L-aspartate 4-semialdehyde + NADPH + H+
-
r
1.1.1.3 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
1.1.1.3 additional information enzyme BsHSD exclusively prefers NADP+ to NAD+ Bacillus subtilis ?
-
-
1.1.1.3 additional information enzyme BsHSD exclusively prefers NADP+ to NAD+ Bacillus subtilis 168 ?
-
-

Subunits

EC Number Subunits Comment Organism
1.1.1.3 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
1.1.1.3 tetramer 4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.3 BsHSD
-
Bacillus subtilis
1.1.1.3 hom
-
Bacillus subtilis
1.1.1.3 HSD
-
Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.3 35 40
-
Bacillus subtilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.3 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]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.3 54.8
-
melting temperature of recombinant enzyme BsHSD Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.3 1.07
-
L-homoserine pH 9.0, 25°C, recombinant enzyme Bacillus subtilis
1.1.1.3 1.1
-
NADP+ pH 9.0, 25°C, recombinant enzyme Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.3 9
-
L-HSE oxidation in the presence of 0.4 M NaCl Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.3 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

EC Number Cofactor Comment Organism Structure
1.1.1.3 NADP+ enzyme BsHSD exclusively prefers NADP+ to NAD+ Bacillus subtilis
1.1.1.3 NADPH
-
Bacillus subtilis

General Information

EC Number General Information Comment Organism
1.1.1.3 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
1.1.1.3 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.3 0.031
-
L-homoserine pH 9.0, 25°C, recombinant enzyme Bacillus subtilis
1.1.1.3 28.2
-
NADP+ pH 9.0, 25°C, recombinant enzyme Bacillus subtilis