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Literature summary extracted from

  • Dobson, R.C.; Devenish, S.R.; Turner, L.A.; Clifford, V.R.; Pearce, F.G.; Jameson, G.B.; Gerrard, J.A.
    Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase (2005), Biochemistry, 44, 13007-13013.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 crystal structure of mutant enzyme R138H and R138A, hanging-drop vapor diffusion method Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.3.3.7 R138A activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns Escherichia coli
4.3.3.7 R138H activity is approximately 0.1% of wild-type activity, Km-value for L-aspartate 4-semialdehyde is significantly higher than the wild-type value, shows the same IC50 values as the wild-type enzyme, but different partial inhibition patterns Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 (S)-lysine mutant enzymes R138H and R138A show the same IC50 values as the wild-type enzyme, but different partial inhibition patterns Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.3.7 0.28
-
 pyruvate mutant enzyme R138H Escherichia coli
4.3.3.7 0.45
-
 pyruvate mutant enzyme R138A Escherichia coli
4.3.3.7 5.1
-
 L-aspartate 4-semialdehyde mutant enzyme R138A Escherichia coli
4.3.3.7 37
-
 L-aspartate 4-semialdehyde mutant enzyme R138H Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.3.7 31000
-
 x * 31000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate Escherichia coli
-
 dihydrodipicolinate + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Escherichia coli P0A6L2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate
-
 Escherichia coli dihydrodipicolinate + H2O
-
 ?
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate branch poit of (S)-lysine biosynthesis Escherichia coli dihydrodipicolinate + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.3.7 ? x * 31000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 DHDPS
-
 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 0.038
-
 pyruvate mutant enzyme R138H Escherichia coli
4.3.3.7 0.038
-
 L-aspartate 4-semialdehyde mutant enzyme R138H Escherichia coli
4.3.3.7 0.149
-
 pyruvate mutant enzyme R138A Escherichia coli
4.3.3.7 0.149
-
 L-aspartate 4-semialdehyde mutant enzyme R138A Escherichia coli