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Literature summary extracted from

  • Chen, H.J.; Ko, T.P.; Lee, C.Y.; Wang, N.C.; Wang, A.H.
    Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase (2009), Structure, 17, 517-529.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.12 expressed in Escherichia coli BL21(DE3) cells Pseudomonas sp.
4.1.1.12 expressed in Escherichia coli BL21(DE3) cells Comamonas testosteroni

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.12 hanging drop vapor diffusion method, using 15% (w/v) PEG4000 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 7.4-8.5) Comamonas testosteroni
4.1.1.12 hanging drop vapor diffusion method, using 40% (w/v) PEG400 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 8.4) Pseudomonas sp.

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.12 E84K/E88K the mutant retains 13% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 K17A the mutant shows 131.2% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 K315A the mutant shows 36.7% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 R37A the mutant shows 10.4% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 R425A the mutant retains 2.5% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 R487A completely inactive mutant Comamonas testosteroni
4.1.1.12 S67A/Y68A/M69A the mutant retains less than 1% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 S67E/Y68E/M69E the mutations produce an inactive dimer Comamonas testosteroni
4.1.1.12 S67R/Y68R/M69R the mutations produce an inactive dimer Comamonas testosteroni
4.1.1.12 Y134F the mutant shows 40.3% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 Y207F the mutant shows 10.7% activity compared to the wild type enzyme Comamonas testosteroni
4.1.1.12 Y441F the mutant shows 40.8% activity compared to the wild type enzyme Comamonas testosteroni

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.12 Comamonas testosteroni Q93QX0
-
-
4.1.1.12 Comamonas testosteroni CCRC 11585 Q93QX0
-
-
4.1.1.12 Pseudomonas sp.
-
strain ATCC 19121
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.12 Ni-NTA column chromatography and HPLC gel filtration Pseudomonas sp.
4.1.1.12 Ni-NTA column chromatography and HPLC gel filtration Comamonas testosteroni

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.12 L-Asp
-
Pseudomonas sp. L-Ala + CO2
-
?
4.1.1.12 L-Asp
-
Comamonas testosteroni L-Ala + CO2
-
?
4.1.1.12 L-Asp
-
Comamonas testosteroni CCRC 11585 L-Ala + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.12 homododecamer x-ray crystallography Pseudomonas sp.
4.1.1.12 homododecamer x-ray crystallography Comamonas testosteroni

Synonyms

EC Number Synonyms Comment Organism
4.1.1.12 Asd
-
Pseudomonas sp.
4.1.1.12 Asd
-
Comamonas testosteroni
4.1.1.12 L-Aspartate beta-decarboxylase
-
Pseudomonas sp.
4.1.1.12 L-Aspartate beta-decarboxylase
-
Comamonas testosteroni

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.12 259
-
L-Asp mutant enzyme Y134F, at pH 5.0 and 37°C Comamonas testosteroni
4.1.1.12 270
-
L-Asp mutant enzyme R37A, at pH 5.0 and 37°C Comamonas testosteroni
4.1.1.12 273
-
L-Asp mutant enzyme Y441F, at pH 5.0 and 37°C Comamonas testosteroni
4.1.1.12 279
-
L-Asp mutant enzyme K315A, at pH 5.0 and 37°C Comamonas testosteroni
4.1.1.12 294
-
L-Asp mutant enzyme Y207F, at pH 5.0 and 37°C Comamonas testosteroni
4.1.1.12 311
-
L-Asp mutant enzyme K17A, at pH 5.0 and 37°C Comamonas testosteroni
4.1.1.12 442
-
L-Asp wild type enzyme, at pH 5.0 and 37°C Comamonas testosteroni

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.12 pyridoxal 5'-phosphate dependent on, pyridoxal 5'-phosphate is bound covalently to Lys315 in the active site Pseudomonas sp.
4.1.1.12 pyridoxal 5'-phosphate dependent on, pyridoxal 5'-phosphate is bound covalently to Lys315 in the active site Comamonas testosteroni