Information on EC 3.5.1.79 - Phthalyl amidase:
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The lowest common taxonomy group for this enzyme is: Xanthobacter agilis

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EC NUMBERCOMMENTARY
3.5.1.79-

RECOMMENDED NAMEGeneOntology No.
Phthalyl amidaseGO:0047418

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
A phthalylamide + H2O = phthalic acid + a substituted amine
show the reaction diagram		mechanismXanthobacter agilis-31905
A phthalylamide + H2O = phthalic acid + a substituted amine
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of linear amides----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
Phthalyl-amide amidohydrolaseIn 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

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Amidase, phthalyl----
o-Phthalyl amidase----

CAS REGISTRY NUMBERCOMMENTARY
169150-79-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Xanthobacter agilis-31905, 31906, 31907, 31908, 31909--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. 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		Xanthobacter agilis--31905, 31906---
2-Carboxybenzoylamine-D-phenylglycine-methylester?
show the reaction diagram		Xanthobacter agilis--31905, 31906---
2-Carboxybenzoylamine-L-Phe-L-Ala?
show the reaction diagram		Xanthobacter agilis--31905, 31906---
N-Phthalamido-L-Asp-L-Phe methyl ester?
show the reaction diagram		Xanthobacter agilis--31907---
o-Phthalyl carbacephemLoracarbef + phthalic acid
show the reaction diagram		Xanthobacter agilis--31905-31905-
[4-[(2-Carboxybenzoyl)amino]-1H-imidazol-1-yl]octanoic acid?
show the reaction diagram		Xanthobacter agilis--31905---
7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-emAspartame + phthalic acid
show the reaction diagram		Xanthobacter agilis-i.e. phthalamindo carbacephem31908---
additional information?-Xanthobacter agilis-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 group31908---
additional information?-Xanthobacter agilis-broad specificity for o-phthalylated amides, absolute requirement for the o-phthalyl protecting group31905---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
No entries in this field

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Cu2+Xanthobacter agilis--31907, 31908 2D-image
iodoacetateXanthobacter agilis--31906, 31907, 31908 2D-image
Mn2+Xanthobacter agilis-slight31907 2D-image
p-hydroxymercuribenzoateXanthobacter agilis--31906, 31907, 31908 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.16-2-carboxybenzoylamine-D-Phe-L-AlaXanthobacter agilis--31906 2D-image
0.56-2-carboxybenzoylamine-D-phenylglycine-methylesterXanthobacter agilis--31906 2D-image
0.23-2-carboxybenzoylamine-L-Phe-L-AlaXanthobacter agilis--31906 2D-image
0.9-7-Phthalamido-3-chloro-4-carboxy-1-carbadethioceph-3-emXanthobacter agilis--31908 2D-image
additional information-additional informationXanthobacter agilis--31909-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.8-2-carboxybenzoylamine-D-Phe-L-AlaXanthobacter agilis--31906 2D-image
4.7-2-carboxybenzoylamine-D-phenylglycine-methylesterXanthobacter agilis--31906 2D-image
2.3-2-carboxybenzoylamine-L-Phe-L-AlaXanthobacter agilis--31906 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
6.3-Xanthobacter agilis--31907
9-Xanthobacter agilis--31905

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.88.4Xanthobacter agilis--31907
8-Xanthobacter agilis--31908

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.59Xanthobacter agilis--31908

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
2834Xanthobacter agilis--31907
30-Xanthobacter agilis--31908

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1050Xanthobacter agilis--31908

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
49900-Xanthobacter agilis-electrospray mass spectrometry31908

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
monomerXanthobacter agilis-1 * 49000, SDS-PAGE; 1 * 49724, calculation from nucleotide sequence31905
monomerXanthobacter agilis-1 * 49900-50000, SDS-PAGE31908, 31909

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
25-Xanthobacter agilis-below, pH 8.2, 48 h, 10% loss of activity31908
35-Xanthobacter agilis-pH 8.2, 48 h, 20% loss of activity31908
40-Xanthobacter agilis-pH 8.2, 48 h, 70% loss of activity31908

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
pH-stability and temperature-stability is improved significantly by increasing ionic strength of the bufferXanthobacter agilis-31905
stability is dependent on the high ionic strength of the bufferXanthobacter agilis-31908
the enzyme stability is optimal at salt concentrations of 0.2 M and aboveXanthobacter agilis-31905
the substrate phthalimido carbacephem stablilizes the enzymeXanthobacter agilis-31905

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Xanthobacter agilis-31907, 31908
large scaleXanthobacter agilis-31905

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Streptomyces lividans and Escherichia coliXanthobacter agilis-31909

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisXanthobacter agilis-alternative chemical route in removing the phthalimido protecting group31905
synthesisXanthobacter agilis-selective deprotection of phthalyl protected amines31906
synthesisXanthobacter agilis-one-step synthesis of the antibiotic loracarbef; selective deprotection of phthalyl protected amines; synthesis of aspartame; 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 group31908

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
31905Black, T.D.; Briggs, B.S.; Evans, R.; Muth, W.L.; Vangala, S.; Zmijewski, M.J.o-Phthalyl amidase in the synthesis of loracarbef: process development using this novel biocatalystBiotechnol. Lett.18875-8801996Xanthobacter agilis-
31906Costello, C.A.; Kreuzman, A.J.; Zmijewski, M.J.Selective deprotection of phthalyl protected aminesTetrahedron Lett.377469-74721996Xanthobacter agilis-
31907Briggs, B.S.; Kreuzman, A.J.; Whitesitt, C.; Yeh, W.K.; Zmijewski, M.Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilisJ. Mol. Catal., B Enzym.253-691996Xanthobacter agilis-
31908Briggs, B.S.; Zmijewski Jr., M.J.Enzyme from microbial sources: phthalyl amidaseUnited States Patent 5,445,9591995Xanthobacter agilis-
31909Queener, S.W.; Zock, J.M.Genes encoding and method of expressing a novel enzyme phthalyl amidaseUnited States Patent 5,543,4971996Xanthobacter agilis-

LINKS TO OTHER DATABASES (specific for EC-Number 3.5.1.79)
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MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)