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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.3 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

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

Inhibitors

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

KM Value [mM]

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

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+ Staphylococcus aureus
-
L-aspartate 4-semialdehyde + NADPH + H+
-
r
1.1.1.3 L-homoserine + NADP+ Staphylococcus aureus COL
-
L-aspartate 4-semialdehyde + NADPH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.3 Staphylococcus aureus A0A0H2WVX4
-
-
1.1.1.3 Staphylococcus aureus COL A0A0H2WVX4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.3 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

EC Number Reaction Comment Organism Reaction ID
1.1.1.3 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)

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

Subunits

EC Number Subunits Comment Organism
1.1.1.3 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
1.1.1.3 More structural basis for the catalytic mechanism of homoserine dehydrogenase, overview Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.3 hom
-
Staphylococcus aureus
1.1.1.3 HSD
-
Staphylococcus aureus
1.1.1.3 SACOL1362
-
Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.3 37
-
-
Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.3 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

EC Number Cofactor Comment Organism Structure
1.1.1.3 NADP+
-
Staphylococcus aureus
1.1.1.3 NADPH
-
Staphylococcus aureus

General Information

EC Number General Information Comment Organism
1.1.1.3 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
1.1.1.3 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
1.1.1.3 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