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Literature summary extracted from

  • Burgess, B.R.; Dobson, R.C.; Bailey, M.F.; Atkinson, S.C.; Griffin, M.D.; Jameson, G.B.; Parker, M.W.; Gerrard, J.A.; Perugini, M.A.
    Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen (2008), J. Biol. Chem., 283, 27598-27603.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 atomic resolution at 1.45 A, crystal structure confirms the dimeric quarternary structure, reveals that the dimerization interface of the MRSA-DHDPS enzyme is more extensive in buried surface area and noncovalent contacts than the equivalent interface in tetrameric DHDPS enzymes from other bacterial species Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 (S)-aspartate 4-semialdehyde
-
Staphylococcus aureus
4.3.3.7 additional information insensitivity to lysine inhibition Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.3.7 0.11
-
pyruvate similar to those of DHDPS enzyme of Escherichia coli Staphylococcus aureus
4.3.3.7 0.22
-
(S)-aspartate 4-semialdehyde similar to those of DHDPS enzyme of Escherichia coli Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate Staphylococcus aureus
-
dihydrodipicolinate + H2O
-
?
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate Staphylococcus aureus MRSA252
-
dihydrodipicolinate + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Staphylococcus aureus Q6GH13 methicillin-resistent MRSA252 strain
-
4.3.3.7 Staphylococcus aureus MRSA252 Q6GH13 methicillin-resistent MRSA252 strain
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.3.7 additional information
-
mechanistic insight into catalysis, structural features and the evolution of quarternary structure, MRSA-DHDPS enzyme exists in a monomer-dimer equilibrium in solution, MRSA-DHDPS dimer is catalytically active Staphylococcus aureus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate
-
Staphylococcus aureus dihydrodipicolinate + H2O
-
?
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate mechanistic insight into catalysis, structural features, evolution of quaternary structure Staphylococcus aureus dihydrodipicolinate + H2O
-
?
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate
-
Staphylococcus aureus MRSA252 dihydrodipicolinate + H2O
-
?
4.3.3.7 (S)-aspartate 4-semialdehyde + pyruvate mechanistic insight into catalysis, structural features, evolution of quaternary structure Staphylococcus aureus MRSA252 dihydrodipicolinate + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 MRSA-DHDPS
-
Staphylococcus aureus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.3.7 70
-
pyruvate ping-pong kinetic mechanism Staphylococcus aureus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.3.3.7 0.07
-
(S)-aspartate 4-semialdehyde substrate inhibition Staphylococcus aureus