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Literature summary for 4.1.1.12 extracted from

  • Phillips, R.S.; Lima, S.; Khristoforov, R.; Sudararaju, B.
    Insights into the mechanism of Pseudomonas dacunhae aspartate beta-decarboxylase from rapid-scanning stopped-flow kinetics (2010), Biochemistry, 49, 5066-5073.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R37A the mutant shows a 5000fold slower kcat value than the wild type enzyme Pseudomonas dacunhae

Organism

Organism UniProt Comment Textmining
Pseudomonas dacunhae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
erythro-beta-hydroxy-DL-Asp the reaction of erythro-beta-hydroxy-DL-Asp with ABDC is at least 16700fold slower than that with L-aspartate Pseudomonas dacunhae ?
-
?
L-aspartate
-
Pseudomonas dacunhae L-alanine + CO2
-
?
succinate
-
Pseudomonas dacunhae ?
-
?
threo-beta-hydroxy-DL-Asp the reaction of threo-beta-hydroxy-DL-Asp with ABDC is at least 1000fold slower than that with L-aspartate Pseudomonas dacunhae ?
-
?

Synonyms

Synonyms Comment Organism
ABDC
-
Pseudomonas dacunhae
Aspartate beta-decarboxylase
-
Pseudomonas dacunhae

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Pseudomonas dacunhae