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Literature summary extracted from

  • Briggs, B.S.; Zmijewski Jr., M.J.
    Enzyme from microbial sources: phthalyl amidase (1995), United States Patent 5,445,959, , .
No PubMed abstract available

Application

EC Number Application Comment Organism
3.5.1.79 synthesis selective deprotection of phthalyl protected amines Xanthobacter agilis
3.5.1.79 synthesis the enzyme catalyzes removal of the phthalyl group from a wide variety of phthalyl-containing compounds with improved yields over processes, exhibits stereochemical selectivity, and eliminates the need for harsh conditions to remove the protecting group Xanthobacter agilis
3.5.1.79 synthesis one-step synthesis of the antibiotic loracarbef Xanthobacter agilis
3.5.1.79 synthesis synthesis of aspartame Xanthobacter agilis

General Stability

EC Number General Stability Organism
3.5.1.79 stability is dependent on the high ionic strength of the buffer Xanthobacter agilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.79 Cu2+
-
Xanthobacter agilis
3.5.1.79 iodoacetate
-
Xanthobacter agilis
3.5.1.79 p-hydroxymercuribenzoate
-
Xanthobacter agilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.79 0.9
-
7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-em
-
Xanthobacter agilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.79 49900
-
electrospray mass spectrometry Xanthobacter agilis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.79 Xanthobacter agilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.79
-
Xanthobacter agilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.79 7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-em i.e. phthalamindo carbacephem Xanthobacter agilis Aspartame + phthalic acid
-
?
3.5.1.79 additional information substrate specificity: hydrolyzes phthalylated amino acids, peptides, beta-lactams, aromatic and aliphatic amines. Substitutions allowed on the phthalyl group include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxyl group Xanthobacter agilis ?
-
?

Subunits

EC Number Subunits Comment Organism
3.5.1.79 monomer 1 * 49900-50000, SDS-PAGE Xanthobacter agilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.79 30
-
-
Xanthobacter agilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.79 10 50
-
Xanthobacter agilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.79 25
-
below, pH 8.2, 48 h, 10% loss of activity Xanthobacter agilis
3.5.1.79 35
-
pH 8.2, 48 h, 20% loss of activity Xanthobacter agilis
3.5.1.79 40
-
pH 8.2, 48 h, 70% loss of activity Xanthobacter agilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.79 8
-
-
Xanthobacter agilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.79 5.5 9
-
Xanthobacter agilis