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Literature summary extracted from

  • Faehnle, C.R.; Blanco, J.; Viola, R.E.
    Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase (2004), Acta Crystallogr. Sect. D, 60, 2320-2324.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.11 about 10 mg/ml pure recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, complexed with oxyanions arsenate or periodate, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 22-24% PEG 4000, 0.2 M ammonium acetate, and Tris-HCl, pH 8.5, soaking of crystals before harvest in a solution containing 26% PEG3350, 0.2 M ammonium acetate, 100 mM periodate or arsenate,0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution Haemophilus influenzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.11 additional information inhibitor binding structure and mechanism Haemophilus influenzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.11 L-4-aspartyl phosphate + NADPH Haemophilus influenzae physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway L-aspartate-4-semialdehyde + phosphate + NADP+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.11 Haemophilus influenzae P44801 gene asd
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.11 L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+ catalytic mechanism, substrate recognition Haemophilus influenzae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.11 L-4-aspartyl phosphate + NADPH physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway Haemophilus influenzae L-aspartate-4-semialdehyde + phosphate + NADP+
-
 r
1.2.1.11 L-aspartate-4-semialdehyde + phosphate + NADP+ formation of an acyl-enzyme intermediate Haemophilus influenzae L-4-aspartyl phosphate + NADPH
-
 r
1.2.1.11 additional information oxyanion binding sites and structures with arsenate and periodate Haemophilus influenzae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.11 ASADH
-
 Haemophilus influenzae
1.2.1.11 aspartate-beta-semialdehyde dehydrogenase
-
 Haemophilus influenzae

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.11 NADP+
-
 Haemophilus influenzae
1.2.1.11 NADPH
-
 Haemophilus influenzae