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Literature summary for 4.3.3.7 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
Search for more literature for 4.3.3.7

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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

Synonyms

Synonyms Comment Organism
MRSA-DHDPS
-
 Staphylococcus aureus

Turnover Number [1/s]

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

Ki Value [mM]

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