BRENDA - Enzyme Database show

The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution

Mirwaldt, C.; Korndoerfer, I.; Huber, R.; J. Mol. Biol. 246, 227-239 (1995)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
4.3.3.7
crystal structure at 2.5 A resolution
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
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
L-aspartate-4-semialdehyde + pyruvate
-
33913
Escherichia coli
dihydrodipicolinate + H2O
-
33913
Escherichia coli
?
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.3.3.7
crystal structure at 2.5 A resolution
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
L-aspartate-4-semialdehyde + pyruvate
-
33913
Escherichia coli
dihydrodipicolinate + H2O
-
33913
Escherichia coli
?