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Literature summary extracted from

  • Wang, N.C.; Lee, C.Y.
    Enhanced transaminase activity of a bifunctional L-aspartate 4-decarboxylase (2007), Biochem. Biophys. Res. Commun., 356, 368-373.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.12 gene asd, DNA and amino acid sequence determination and analysis, sequence comparisons Pseudomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.1 Y225R/R292K/R386A the mutation converts its activity into an aspartate 4-decarboxylase Escherichia coli
4.1.1.12 D360P site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme Pseudomonas sp.
4.1.1.12 F204W site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but highly increased aminotransferase compared to the wild-type enzyme Pseudomonas sp.
4.1.1.12 H123Y site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity and slightly increased aminotransferase compared to the wild-type enzyme Pseudomonas sp.
4.1.1.12 H337R site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but similar aminotransferase compared to the wild-type enzyme Pseudomonas sp.
4.1.1.12 K347R site-directed mutagenesis, the mutant shows similar 4-decarboxylation activity but reduced aminotransferase compared to the wild-type enzyme Pseudomonas sp.
4.1.1.12 M178L site-directed mutagenesis, the mutant shows reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme Pseudomonas sp.
4.1.1.12 V475L site-directed mutagenesis, the mutant shows slightly reduced 4-decarboxylation activity but unaltered aminotransferase compared to the wild-type enzyme Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.12 L-aspartate Pseudomonas sp.
-
L-alanine + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.1 Escherichia coli P00509
-
-
4.1.1.12 Pseudomonas sp. Q53IZ1 strain ATCC 19121
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.1 0.06
-
wild type enzyme, at 37°C Escherichia coli
4.1.1.12 additional information
-
4-decarboxylation activity and aminotransferase activity of mutant enzymes, overview Pseudomonas sp.
4.1.1.12 0.06
-
recombinant wild-type enzyme, aminotransferase activity Pseudomonas sp.
4.1.1.12 128.8
-
recombinant wild-type enzyme, 4-decarboxylation activity Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.1 L-aspartate + 2-oxoglutarate
-
Escherichia coli oxaloacetate + L-glutamate
-
?
4.1.1.12 L-aspartate
-
Pseudomonas sp. L-alanine + CO2
-
?
4.1.1.12 additional information Asd is a bifunctional enzyme performing decarboxylation and aminotransferase activities on L-aspartate Pseudomonas sp. ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.1 AspAT
-
Escherichia coli
4.1.1.12 Asd
-
Pseudomonas sp.
4.1.1.12 L-aspartate 4-decarboxylase
-
Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.12 37
-
assay at Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.12 5
-
assay at Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.12 pyridoxal 5'-phosphate dependent on Pseudomonas sp.