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

BRENDA support

Literature summary extracted from

  • Domigan, L.J.; Scally, S.W.; Fogg, M.J.; Hutton, C.A.; Perugini, M.A.; Dobson, R.C.; Muscroft-Taylor, A.C.; Gerrard, J.A.; Devenish, S.R.
    Characterisation of dihydrodipicolinate synthase (DHDPS) from Bacillus anthracis (2009), Biochim. Biophys. Acta, 1794, 1510-1516.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.3.3.7 L-methionine at 10 mM 112% activity, at 100 mM 111% activity Escherichia coli
4.3.3.7 meso-diaminopimelate at 1 mM 108% activity, at 10 mM 122% activity Escherichia coli
4.3.3.7 additional information meso-diaminopimelate has no effect Bacillus anthracis

Application

EC Number Application Comment Organism
4.3.3.7 drug development DHDPS is a potential antibiotic target Bacillus anthracis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.7 plasmid pB3935 containing a His-tagged copy of the dapA2 gene and a gene conferring kanamycin resistance, transformed into Escherichia coli BL21(DE3) for protein overexpression Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 L-aspartate 4-semialdehyde DHDPS is subject to substrate inhibition by L-aspartate 4-semialdehyde Bacillus anthracis
4.3.3.7 L-lysine at 1 mM 23% residual activity, at 100 mM 13% residual activity Escherichia coli
4.3.3.7 L-methionine at 10 or 100 mM 80% residual activity Bacillus anthracis
4.3.3.7 L-threonine at 100 mM 40% residual activity Bacillus anthracis
4.3.3.7 L-threonine at 100 mM 23% residual activity, at 100 mM 33% residual activity Escherichia coli
4.3.3.7 additional information is not inhibited by 1-100 mM L-lysine or L-isoleucine Bacillus anthracis
4.3.3.7 additional information 1-100 mM L-isoleucine has no effect Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.3.7 0.18
-
 L-aspartate 4-semialdehyde
-
 Bacillus anthracis
4.3.3.7 0.43
-
 pyruvate
-
 Bacillus anthracis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.3.7 32290
-
 mass spectrometry Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Bacillus anthracis Q81WN7
-
-
4.3.3.7 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7 to homogeneity Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate active sites are similiar to Bacillus anthracis DHDPS Escherichia coli dihydrodipicolinate + 2 H2O
-
 ?
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate active sites are similiar to Escherichia coli DHDPS Bacillus anthracis dihydrodipicolinate + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DapA2
-
 Bacillus anthracis
4.3.3.7 DHDPS
-
 Escherichia coli
4.3.3.7 DHDPS
-
 Bacillus anthracis
4.3.3.7 dihydrodipicolinate synthase
-
 Escherichia coli
4.3.3.7 dihydrodipicolinate synthase
-
 Bacillus anthracis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.3.3.7 59.8
-
 is thermally stabilised by the first substrate, pyruvate, to a greater extent than its Escherichia coli counterpart Bacillus anthracis
4.3.3.7 61.3
-
 is thermally stabilised by the first substrate, pyruvate Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.3.7 76
-
 pyruvate
-
 Bacillus anthracis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.3.7 5.4
-
 L-aspartate 4-semialdehyde
-
 Bacillus anthracis