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Literature summary for 3.5.1.4 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

Application Comment Organism
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]

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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