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Literature summary for 1.2.1.11 extracted from

  • Hadfield, A.; Kryger, G.; Ouyang, J.; Petsko, G.A.; Ringe, D.; Viola, R.
    Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis (1999), J. Mol. Biol., 289, 991-1002.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
using the hanging drop method Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-4-aspartyl phosphate + NADPH Escherichia coli
-
L-aspartate 4-semialdehyde + phosphate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9Q9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-4-aspartyl phosphate + NADPH
-
Escherichia coli L-aspartate 4-semialdehyde + phosphate + NADP+
-
?
L-aspartate 4-semialdehyde + phosphate + NADP+
-
Escherichia coli L-4-aspartyl phosphate + NADPH
-
r

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli
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

Cofactor Comment Organism Structure
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli