BRENDA - Enzyme Database show

Lysine and threonine biosynthesis from aspartate contributes to Staphylococcus aureus growth in calf serum

Oogai, Y.; Yamaguchi, M.; Kawada-Matsuo, M.; Sumitomo, T.; Kawabata, S.; Komatsuzawa, H.; Appl. Environ. Microbiol. 82, 6150-6157 (2016)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.2.1.11
additional information
construction of and screening of a library of 2914 transposon-insertional mutants in the Staphylococcus aureus MW2 strain, identification of aspartate semialdehyde dehydrogenase (asd)-inactivated mutant, and inactivated mutants of lysA and thrC defective in lysine and threonine bioynthesis. Identification of Tn551 insertion sites, the Tn551 insertion sites of M3-91 and M17-9 are 276 bp and 347 bp from the initiation of the asd gene, respectively
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Staphylococcus aureus
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Staphylococcus aureus MW2
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Staphylococcus aureus
-
methicillin resistant
-
1.2.1.11
Staphylococcus aureus MW2
-
methicillin resistant
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741702
Staphylococcus aureus
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741702
Staphylococcus aureus MW2
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Staphylococcus aureus
1.2.1.11
NADPH
-
Staphylococcus aureus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Staphylococcus aureus
1.2.1.11
NADPH
-
Staphylococcus aureus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.2.1.11
additional information
construction of and screening of a library of 2914 transposon-insertional mutants in the Staphylococcus aureus MW2 strain, identification of aspartate semialdehyde dehydrogenase (asd)-inactivated mutant, and inactivated mutants of lysA and thrC defective in lysine and threonine bioynthesis. Identification of Tn551 insertion sites, the Tn551 insertion sites of M3-91 and M17-9 are 276 bp and 347 bp from the initiation of the asd gene, respectively
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Staphylococcus aureus
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
Staphylococcus aureus MW2
-
L-4-aspartyl phosphate + NADPH + H+
-
-
r
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741702
Staphylococcus aureus
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
741702
Staphylococcus aureus MW2
L-4-aspartyl phosphate + NADPH + H+
-
-
-
r
General Information
EC Number
General Information
Commentary
Organism
1.2.1.11
malfunction
the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
Staphylococcus aureus
1.2.1.11
metabolism
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
Staphylococcus aureus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.1.11
malfunction
the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
Staphylococcus aureus
1.2.1.11
metabolism
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
Staphylococcus aureus