BRENDA - Enzyme Database show

Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis

Hadfield, A.; Kryger, G.; Ouyang, J.; Petsko, G.A.; Ringe, D.; Viola, R.; J. Mol. Biol. 289, 991-1002 (1999)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
1.2.1.11
using the hanging drop method
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH
Escherichia coli
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
Escherichia coli
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Escherichia coli
P0A9Q9
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.2.1.11
-
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH
-
390199
Escherichia coli
L-aspartate 4-semialdehyde + phosphate + NADP+
-
390199
Escherichia coli
-
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
390199
Escherichia coli
L-4-aspartyl phosphate + NADPH
-
390199
Escherichia coli
r
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
-
Escherichia coli
1.2.1.11
More
the asymmetric unit contains three subunits: one complete dimer and a monomer which comes from a dimer lying along the crystallographic 2fold axis
Escherichia coli
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Escherichia coli
1.2.1.11
NADPH
-
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Escherichia coli
1.2.1.11
NADPH
-
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.2.1.11
using the hanging drop method
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
1.2.1.11
L-4-aspartyl phosphate + NADPH
Escherichia coli
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
Escherichia coli
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.11
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH
-
390199
Escherichia coli
L-aspartate 4-semialdehyde + phosphate + NADP+
-
390199
Escherichia coli
-
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
-
390199
Escherichia coli
L-4-aspartyl phosphate + NADPH
-
390199
Escherichia coli
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
-
Escherichia coli
1.2.1.11
More
the asymmetric unit contains three subunits: one complete dimer and a monomer which comes from a dimer lying along the crystallographic 2fold axis
Escherichia coli