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Literature summary for 4.1.1.12 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
Search for more literature for 4.1.1.12

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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
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

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Turnover Number [1/s]

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

Cofactor

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