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Literature summary for 3.5.1.79 extracted from
- Enzyme from microbial sources: phthalyl amidase (1995), United States Patent 5,445,959, , .
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | selective deprotection of phthalyl protected amines | Xanthobacter agilis |
| 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 |
| synthesis | one-step synthesis of the antibiotic loracarbef | Xanthobacter agilis |
| synthesis | synthesis of aspartame | Xanthobacter agilis |
General Stability
| General Stability | Organism |
|---|---|
| stability is dependent on the high ionic strength of the buffer | Xanthobacter agilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | - |
Xanthobacter agilis |  |
| iodoacetate | - |
Xanthobacter agilis | |
| p-hydroxymercuribenzoate | - |
Xanthobacter agilis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.9 | - |
7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-em | - |
Xanthobacter agilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 49900 | - |
electrospray mass spectrometry | Xanthobacter agilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Xanthobacter agilis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Xanthobacter agilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-em | i.e. phthalamindo carbacephem | Xanthobacter agilis | Aspartame + phthalic acid | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 49900-50000, SDS-PAGE | Xanthobacter agilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
- |
Xanthobacter agilis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 50 | - |
Xanthobacter agilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
below, pH 8.2, 48 h, 10% loss of activity | Xanthobacter agilis |
| 35 | - |
pH 8.2, 48 h, 20% loss of activity | Xanthobacter agilis |
| 40 | - |
pH 8.2, 48 h, 70% loss of activity | Xanthobacter agilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Xanthobacter agilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 9 | - |
Xanthobacter agilis |
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