Information on EC 3.5.1.79 - Phthalyl amidase

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The expected taxonomic range for this enzyme is: Xanthobacter agilis

EC NUMBER
COMMENTARY
3.5.1.79
-
RECOMMENDED NAME
GeneOntology No.
Phthalyl amidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
A phthalylamide + H2O = phthalic acid + a substituted amine
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amides
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Phthalyl-amide amidohydrolase
In the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, beta-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Amidase, phthalyl
-
-
-
-
o-Phthalyl amidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
169150-79-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Carboxybenzoylamine-D-Phe-L-Ala
?
show the reaction diagram
-
-
-
-
-
2-Carboxybenzoylamine-D-phenylglycine-methylester
?
show the reaction diagram
-
-
-
-
-
2-Carboxybenzoylamine-L-Phe-L-Ala
?
show the reaction diagram
-
-
-
-
-
N-Phthalamido-L-Asp-L-Phe methyl ester
?
show the reaction diagram
-
-
-
-
-
o-Phthalyl carbacephem
Loracarbef + phthalic acid
show the reaction diagram
-
-
-
-
[4-[(2-Carboxybenzoyl)amino]-1H-imidazol-1-yl]octanoic acid
?
show the reaction diagram
-
-
-
-
-
7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-em
Aspartame + phthalic acid
show the reaction diagram
-
i.e. phthalamindo carbacephem
-
-
-
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
-
-
-
additional information
?
-
-
broad specificity for o-phthalylated amides, absolute requirement for the o-phthalyl protecting group
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
-
slight
p-hydroxymercuribenzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
2-carboxybenzoylamine-D-Phe-L-Ala
-
-
0.56
2-carboxybenzoylamine-D-phenylglycine-methylester
-
-
0.23
2-carboxybenzoylamine-L-Phe-L-Ala
-
-
0.9
7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-em
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
2-carboxybenzoylamine-D-Phe-L-Ala
-
-
4.7
2-carboxybenzoylamine-D-phenylglycine-methylester
-
-
2.3
2-carboxybenzoylamine-L-Phe-L-Ala
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 8.4
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49900
-
electrospray mass spectrometry
31908
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 49000, SDS-PAGE, 1 * 49724, calculation from nucleotide sequence
monomer
-
1 * 49900-50000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
below, pH 8.2, 48 h, 10% loss of activity
31908
35
-
pH 8.2, 48 h, 20% loss of activity
31908
40
-
pH 8.2, 48 h, 70% loss of activity
31908
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pH-stability and temperature-stability is improved significantly by increasing ionic strength of the buffer
-
stability is dependent on the high ionic strength of the buffer
-
the enzyme stability is optimal at salt concentrations of 0.2 M and above
-
the substrate phthalimido carbacephem stablilizes the enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
large scale
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces lividans and Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
alternative chemical route in removing the phthalimido protecting group
synthesis
-
selective deprotection of phthalyl protected amines
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, one-step synthesis of the antibiotic loracarbef, synthesis of aspartame