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Literature summary extracted from

  • Bhatia, R.; Bhatia, S.; Kumar, V.; Bhalla, T.
    Bi-substrate kinetic analysis of acyl transfer activity of purified amidase from Pseudomonas putida BR-1 (2015), Catal. Lett., 145, 1033-1040.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.5.1.4 synthesis the enzyme enzyme has very high potential for biotransformation of N-substituted aromatic amides and for the production of a variety of hydroxamic acids Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.4 48000
-
 1 * 55000, alpha-subunit, + 1 * 48000, beta-subunit, SDS-PAGE Pseudomonas putida
3.5.1.4 55000
-
 1 * 55000, alpha-subunit, + 1 * 48000, beta-subunit, SDS-PAGE Pseudomonas putida
3.5.1.4 128000
-
 native PAGE Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.4 Pseudomonas putida
-
 isolated from rhizosphere of cyanogenic plant Circium vulgare
-
3.5.1.4 Pseudomonas putida BR-1
-
 isolated from rhizosphere of cyanogenic plant Circium vulgare
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.4 native enzyme 2.9fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.4 additional information the enzyme also shows acyl transfer activity, ATA, forming nicotinyl hydroxamic acid and ammonia from nicotinamide and hydroxylamine, kinetics and substrate specificity, detailed overview. The acyl transfer activity of the amidase from Pseudomonas putida BR-1 rapidly catalyzes the biotransformation of short chain amides, i.e. acetamide and propionamide. Unsaturated amides, i.e. acrylamide and methacrylamide act as good substrates while amides having bulky side chain, i.e. L-tryptophanamide and DL-phenylglycinamide are poor substrates Pseudomonas putida ?
-
 ?
3.5.1.4 additional information the enzyme also shows acyl transfer activity, ATA, forming nicotinyl hydroxamic acid and ammonia from nicotinamide and hydroxylamine, kinetics and substrate specificity, detailed overview. The acyl transfer activity of the amidase from Pseudomonas putida BR-1 rapidly catalyzes the biotransformation of short chain amides, i.e. acetamide and propionamide. Unsaturated amides, i.e. acrylamide and methacrylamide act as good substrates while amides having bulky side chain, i.e. L-tryptophanamide and DL-phenylglycinamide are poor substrates Pseudomonas putida BR-1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.4 dimer 1 * 55000, alpha-subunit, + 1 * 48000, beta-subunit, SDS-PAGE Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.4 50
-
 acyl transfer activity Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.4 7.5
-
 acyl transfer activity Pseudomonas putida

General Information

EC Number General Information Comment Organism
3.5.1.4 evolution the enzyme is a member of the nitrilase superfamily Pseudomonas putida