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Literature summary for 4.1.1.76 extracted from

  • Matoishi, K.; Ueda, M.; Miyamoto, K.; Ohta, H.
    Mechanism of asymmetric decarboxylation of alpha-aryl-alpha-methylmalonate catalyzed by arylmalonate decarboxylase originated from Alcaligenes bronchisepticus (2004), J. Mol. Catal. B, 27, 161-168.
No PubMed abstract available
Search for more literature for 4.1.1.76

Protein Variants

Protein Variants Comment Organism
C188S in contrast to the bellshaped pH profile of the wild-type enzyme, the activity of the mutant enzyme C188S retains its full activity from pH 6.0 to pH 11.0 Bordetella bronchiseptica

Inhibitors

Inhibitors Comment Organism Structure
alpha-Bromophenylacetic acid
-
 Bordetella bronchiseptica

Organism

Organism UniProt Comment Textmining
Bordetella bronchiseptica Q05115 KU 1201
-
Bordetella bronchiseptica KU 1201 Q05115 KU 1201
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bordetella bronchiseptica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Phenylmalonate
-
 Bordetella bronchiseptica Phenylacetate + CO2
-
 ?
Phenylmalonate
-
 Bordetella bronchiseptica KU 1201 Phenylacetate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
AMDase
-
 Bordetella bronchiseptica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 11 activity of mutant enzyme C188S retains maximal activity from pH 6.0 to pH 11., substrate: phenylmalonate Bordetella bronchiseptica
8
-
 wild-type enzyme, substrate: phenylmalonate Bordetella bronchiseptica

pH Range

pH Minimum pH Maximum Comment Organism
5 9.5 pH 5.0: about 50% of maximal activity, pH 9.5: about 55% of maximal activity, substrate: phenylmalonate, wild-type enzyme Bordetella bronchiseptica
6 11 activity of mutant enzyme C188S retains maximal activity from pH 6.0 to pH 11.0, substrate: phenylmalonate Bordetella bronchiseptica