Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.3 extracted from

  • Navratna, V.; Reddy, G.; Gopal, B.
    Structural basis for the catalytic mechanism of homoserine dehydrogenase (2015), Acta Crystallogr. Sect. D, 71, 1216-1225.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene hom, recombinant expression of His-tagged wild-type and mutant enzymes in Echerichia coli strain Rosetta (DE3) pLysS Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
K105A site-directed double-primer PCR mutagenesis Staphylococcus aureus
K105R site-directed double-primer PCR mutagenesis Staphylococcus aureus
K205A site-directed double-primer PCR mutagenesis Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
L-serine allosteric inhibitor Staphylococcus aureus
L-threonine allosteric inhibitor Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic profile Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-homoserine + NADP+ Staphylococcus aureus
-
L-aspartate 4-semialdehyde + NADPH + H+
-
r
L-homoserine + NADP+ Staphylococcus aureus COL
-
L-aspartate 4-semialdehyde + NADPH + H+
-
r

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus A0A0H2WVX4
-
-
Staphylococcus aureus COL A0A0H2WVX4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration Staphylococcus aureus

Reaction

Reaction Comment Organism Reaction ID
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-homoserine + NADP+
-
Staphylococcus aureus L-aspartate 4-semialdehyde + NADPH + H+
-
r
L-homoserine + NADP+
-
Staphylococcus aureus COL L-aspartate 4-semialdehyde + NADPH + H+
-
r

Subunits

Subunits Comment Organism
homodimer the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview Staphylococcus aureus
More structural basis for the catalytic mechanism of homoserine dehydrogenase, overview Staphylococcus aureus

Synonyms

Synonyms Comment Organism
hom
-
Staphylococcus aureus
HSD
-
Staphylococcus aureus
SACOL1362
-
Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
the catalytic activity of the enzyme for the conversion of L-homoserine to L-aspartate 4-semialdehyde (the reverse reaction) is enhanced at basic pH Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Staphylococcus aureus
NADPH
-
Staphylococcus aureus

General Information

General Information Comment Organism
metabolism homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine Staphylococcus aureus
additional information structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview Staphylococcus aureus
physiological function the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine Staphylococcus aureus