BRENDA - Enzyme Database show

Structure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogen

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.; J. Biol. Chem. 283, 27598-27603 (2008)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
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
Commentary
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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]
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
-
693141
Staphylococcus aureus
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
mechanistic insight into catalysis, structural features, evolution of quaternary structure
693141
Staphylococcus aureus
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
-
693141
Staphylococcus aureus MRSA252
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
mechanistic insight into catalysis, structural features, evolution of quaternary structure
693141
Staphylococcus aureus MRSA252
dihydrodipicolinate + H2O
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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
Commentary
Organism
Structure
4.3.3.7
0.07
-
(S)-aspartate 4-semialdehyde
substrate inhibition
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
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 (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
(S)-aspartate 4-semialdehyde
-
Staphylococcus aureus
4.3.3.7
additional information
insensitivity to lysine inhibition
Staphylococcus aureus
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.07
-
(S)-aspartate 4-semialdehyde
substrate inhibition
Staphylococcus aureus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
-
693141
Staphylococcus aureus
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
mechanistic insight into catalysis, structural features, evolution of quaternary structure
693141
Staphylococcus aureus
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
-
693141
Staphylococcus aureus MRSA252
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
mechanistic insight into catalysis, structural features, evolution of quaternary structure
693141
Staphylococcus aureus MRSA252
dihydrodipicolinate + H2O
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.3.3.7
70
-
pyruvate
ping-pong kinetic mechanism
Staphylococcus aureus