BRENDA - Enzyme Database show

The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate

Devenish, S.R.; Gerrard, J.A.; Jameson, G.B.; Dobson, R.C.; Acta Crystallogr. Sect. F 64, 1092-1095 (2008)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.3.3.7
expressed in Escherichia coli XL-1 Blue harbouring the plasmid pJG001
Escherichia coli
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
examination of the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, data-collection and refinement statistics
Escherichia coli
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
Escherichia coli
-
dihydrodipicolinate + H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Escherichia coli
P0A6L2
-
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
4.3.3.7
additional information
-
attempt to examine the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, solution of the protein structure indicates that pyruvate rather than oxaloacetic acid bounds in the active site, decarboxylation of oxaloacetate not catalysed by DHDPS, rate of pyruvate production independent of DHDPS concentration, indicating that the decarboxylation of oxaloacetate is occurring by a spontaneous and enzyme-independent mechanism, confirmed by kinetic analysis
Escherichia coli
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
-
690252
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
biosynthesis of (S)-lysine and meso-diaminopimelate
690252
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.3.3.7
7.6
-
assay at, measured using a coupled assay with lactate dehydrogenase to detect pyruvate production
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
expressed in Escherichia coli XL-1 Blue harbouring the plasmid pJG001
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
examination of the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, data-collection and refinement statistics
Escherichia coli
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
Escherichia coli
-
dihydrodipicolinate + H2O
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
4.3.3.7
additional information
-
attempt to examine the specificity of the active site of DHDPS, co-crystallization with the substrate analogue oxaloacetate, solution of the protein structure indicates that pyruvate rather than oxaloacetic acid bounds in the active site, decarboxylation of oxaloacetate not catalysed by DHDPS, rate of pyruvate production independent of DHDPS concentration, indicating that the decarboxylation of oxaloacetate is occurring by a spontaneous and enzyme-independent mechanism, confirmed by kinetic analysis
Escherichia coli
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
-
690252
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
4.3.3.7
(S)-aspartate 4-semialdehyde + pyruvate
biosynthesis of (S)-lysine and meso-diaminopimelate
690252
Escherichia coli
dihydrodipicolinate + H2O
-
-
-
?
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.3.3.7
7.6
-
assay at, measured using a coupled assay with lactate dehydrogenase to detect pyruvate production
Escherichia coli