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Literature summary extracted from

  • Blanco, J.; Moore, R.A.; Faehnle, C.R.; Coe, D.M.; Viola, R.E.
    The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase (2004), Acta Crystallogr. Sect. D, 60, 1388-1395.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.11 expression of wild-type and mutant enzymes Haemophilus influenzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.11 10 mg/ml purified recombinant wild-type and mutant enzymes free or in complex with the substrates, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, by hanging drop vapour diffusion, 20°C, mixed with equal volume of precipitant solution containing 22-24% PEG 3350, and 0.2 M ammonium acetate, crystals are soaked for 1 h in a solution containing 2 mM aspartate-beta-semialdehyde or 100 mM phosphate, 26% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at about 2.0 A resolution Haemophilus influenzae

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.11 E243D site-directed mutagenesis, unaltered Km for the substrates but 8fold increased Km for cofactor NADP+, active site structural alterations Haemophilus influenzae
1.2.1.11 K246R site-directed mutagenesis, mutation of a putative phosphate binding residue, unaltered substrate Km, active site structural alterations Haemophilus influenzae
1.2.1.11 R103K site-directed mutagenesis, adversely affected interaction between enzyme and phosphate, active site structural alterations Haemophilus influenzae
1.2.1.11 R103L site-directed mutagenesis, altered interaction between enzyme and phosphate, active site structural alterations Haemophilus influenzae
1.2.1.11 R270K site-directed mutagenesis, active site mutant, unaltered substrate Km, active site structural alterations Haemophilus influenzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.11 0.03
-
 L-aspartate-4-semialdehyde recombinant mutant R103L Haemophilus influenzae
1.2.1.11 0.1
-
 L-aspartate-4-semialdehyde recombinant mutant R103K and mutant K246L Haemophilus influenzae
1.2.1.11 0.11
-
 NADP+ recombinant mutant R103L Haemophilus influenzae
1.2.1.11 0.17
-
 NADP+ recombinant mutant R270K Haemophilus influenzae
1.2.1.11 0.2
-
 NADP+ recombinant wild-type enzyme Haemophilus influenzae
1.2.1.11 0.2
-
 L-aspartate-4-semialdehyde recombinant wild-type enzyme and mutant E243D Haemophilus influenzae
1.2.1.11 0.4
-
 L-aspartate-4-semialdehyde recombinant mutant R270K Haemophilus influenzae
1.2.1.11 0.6
-
 NADP+ recombinant mutant K246L Haemophilus influenzae
1.2.1.11 0.7
-
 NADP+ recombinant mutant R103K Haemophilus influenzae
1.2.1.11 1
-
 phosphate recombinant mutant K246L Haemophilus influenzae
1.2.1.11 1.5
-
 phosphate recombinant mutant E243D Haemophilus influenzae
1.2.1.11 1.6
-
 phosphate recombinant wild-type enzyme Haemophilus influenzae
1.2.1.11 1.6
-
 NADP+ recombinant mutant E243D Haemophilus influenzae
1.2.1.11 1.9
-
 phosphate recombinant mutant R270K Haemophilus influenzae
1.2.1.11 36.6
-
 phosphate recombinant mutant R103K Haemophilus influenzae
1.2.1.11 240
-
 phosphate recombinant mutant R103L 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-aspartate-4-semialdehyde + phosphate + NADP+ Haemophilus influenzae reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid L-4-aspartyl phosphate + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.11 Haemophilus influenzae
-
 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, role of substrate binding groups, residues Arg270, Glu243, Arg103, and Lys246 are involved Haemophilus influenzae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.11 L-aspartate-4-semialdehyde + phosphate + NADP+ reductive dephosphorylation in the aspartate biosynthetic pathway, aspartate-beta-semialdehydr is the key intermediate in biosynthesis of diaminopimelic acid Haemophilus influenzae L-4-aspartyl phosphate + NADPH
-
 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

Synonyms

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.11 additional information
-
 stability of recombinant wild-type and mutant enzymes, oveview Haemophilus influenzae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.11 0.24
-
 L-aspartate-4-semialdehyde recombinant mutant R103L Haemophilus influenzae
1.2.1.11 0.4
-
 L-aspartate-4-semialdehyde recombinant mutant R270K Haemophilus influenzae
1.2.1.11 1.2
-
 L-aspartate-4-semialdehyde recombinant mutant R103K Haemophilus influenzae
1.2.1.11 4
-
 L-aspartate-4-semialdehyde recombinant mutant E243D Haemophilus influenzae
1.2.1.11 11
-
 L-aspartate-4-semialdehyde recombinant mutant K246L Haemophilus influenzae
1.2.1.11 330
-
 L-aspartate-4-semialdehyde recombinant wild-type enzyme Haemophilus influenzae

Cofactor

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