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aculeacin A + H2O
? + palmitic acid
-
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
echinocandin A + H2O
cyclo-hexapeptide + linoleic acid
echinocandin C + H2O
cyclo-hexapeptide + linoleic acid
echinocandin D + H2O
cyclo-hexapeptide + linoleic acid
penicillin dihydroF + H2O
6-aminopenicillanic acid + hexanoic acid
-
-
-
-
?
penicillin dihydroF + H2O
?
-
-
-
-
?
penicillin F + H2O
6-aminopenicillanic acid + (3E)-hex-3-enoic acid
-
-
-
-
?
penicillin F + H2O
?
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin K + H2O
6-aminopenicillanic acid + octanoic acid
-
-
-
-
?
penicillin K + H2O
?
-
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
-
?
additional information
?
-
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
preferred substrate
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
catalyzes deacylation of aculeacin A
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
catalyzes deacylation of aculeacin A
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
-
-
-
?
aculeacin A + H2O
cyclo-hexapeptide + palmitic acid
preferred substrate
-
-
?
echinocandin A + H2O
cyclo-hexapeptide + linoleic acid
-
-
-
?
echinocandin A + H2O
cyclo-hexapeptide + linoleic acid
-
neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
echinocandin A + H2O
cyclo-hexapeptide + linoleic acid
-
catalyzes deacylation of echinocandin A
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
echinocandin A + H2O
cyclo-hexapeptide + linoleic acid
-
-
-
?
echinocandin C + H2O
cyclo-hexapeptide + linoleic acid
-
neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
echinocandin C + H2O
cyclo-hexapeptide + linoleic acid
-
catalyzes deacylation of echinocandin C
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
echinocandin D + H2O
cyclo-hexapeptide + linoleic acid
-
neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
echinocandin D + H2O
cyclo-hexapeptide + linoleic acid
-
catalyzes deacylation of echinocandin D
deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents
?
penicillin G + H2O
?
-
-
-
?
penicillin G + H2O
?
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
hydrolyzes echinocandin type antibiotics: presumably cyclo-hexapeptides with a long fatty acid side chain, consisting of threonine, hydroxyproline, and several unusual amino acids, the fatty acid constituents may be linoleic, myristic, or palmitic acid
-
-
?
additional information
?
-
-
no significant activity with ampicillin, tunicamycin, colistin, lankacidin C or blasticidin S
-
-
?
additional information
?
-
-
enzyme hydrolyzes the acyl moieties of antifungal echinocandin antibiotics, efficiently hydrolyzes penicillin V and natural aliphatic penicillins to yield 6-aminopenicillanic acid
-
-
?
additional information
?
-
a cephalosporin acylase (EC 3.5.1.93) enzyme mutant with binding pocket altered for the binding of long acyl chain shows lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
hydrolyzes echinocandin type antibiotics: presumably cyclo-hexapeptides with a long fatty acid side chain, consisting of threonine, hydroxyproline, and several unusual amino acids, the fatty acid constituents may be linoleic, myristic, or palmitic acid
-
-
?
additional information
?
-
-
no significant activity with ampicillin, tunicamycin, colistin, lankacidin C or blasticidin S
-
-
?
additional information
?
-
a cephalosporin acylase (EC 3.5.1.93) enzyme mutant with binding pocket altered for the binding of long acyl chain shows lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme
-
-
?
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physiological function
-
enzyme hydrolyzes the acyl moieties of antifungal echinocandin antibiotics, efficiently hydrolyzes penicillin V and natural aliphatic penicillins to yield 6-aminopenicillanic acid
evolution
the antibiotic acylases belong to the N-terminal nucleophile hydrolase superfamily
evolution
-
the antibiotic acylases belong to the N-terminal nucleophile hydrolase superfamily
-
metabolism
antibiotic acylases cephalosporin acylase (EC 3.5.1.93) and penicillin G acylase (EC 3.5.1.11) catalyze the deacylation of beta-lactam antibiotics, while aculeacin A acylase (AAC) is known to be an alternative acylase class catalyzing the deacylation of echinocandin or cyclic lipopeptide antibiotic compounds
metabolism
-
antibiotic acylases cephalosporin acylase (EC 3.5.1.93) and penicillin G acylase (EC 3.5.1.11) catalyze the deacylation of beta-lactam antibiotics, while aculeacin A acylase (AAC) is known to be an alternative acylase class catalyzing the deacylation of echinocandin or cyclic lipopeptide antibiotic compounds
-
additional information
three-dimensional homology models of AAC are constructed, and docking simulation with substrate ligands is performed for AAC. Enzyme AAC has the deep narrow binding pocket for the long-chain fatty acyl group of the echinocandin molecule
additional information
-
three-dimensional homology models of AAC are constructed, and docking simulation with substrate ligands is performed for AAC. Enzyme AAC has the deep narrow binding pocket for the long-chain fatty acyl group of the echinocandin molecule
-
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19000
-
1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits
19100
-
1 * 60300 + 1 * 19100, two dissimilar subunits, calculated from nucleotide sequence
38000
-
HPLC gel filtration, the large discrepancy between the molecular weight estimated by HPLC and that estimated by SDS-PAGE is due to the particularly high pI of the enzyme: the molecular weight of acylase should be 74000 Da, the sum of the values of the two subunits obtained by SDS-PAGE
55000
-
1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits
60300
-
1 * 60300 + 1 * 19100, two dissimilar subunits, calculated from nucleotide sequence
84070
-
precursor peptide of aculeacin A acylase, calculated from nucleotide sequence
87000
-
precursor peptide of aculeacin A acylase, gel filtration and SDS-PAGE
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dimer
-
-
dimer
-
1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits
dimer
-
1 * 60300 + 1 * 19100, two dissimilar subunits, calculated from nucleotide sequence
dimer
-
two subunits which are associated by a bond other than disulfide bond
dimer
-
1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits
-
dimer
-
two subunits which are associated by a bond other than disulfide bond
-
dimer
-
1 * 60300 + 1 * 19100, two dissimilar subunits, calculated from nucleotide sequence
-
monomer
-
1 * 87000, SDS-PAGE and gel filtration, precursor peptide of aculeacin A acylase
monomer
-
1 * 87000, SDS-PAGE and gel filtration, precursor peptide of aculeacin A acylase
-
additional information
-
the 87000 Da enzyme precursor protein is processed post-translationally at 37°C, 0.1% SDS for 1 h to 60000 Da and 19000 Da peptides by its own proteolytic activity
additional information
-
enzyme is translated as single precursor polypeptide and then processed by proteolytic processing to the active form consisting of two subunits
additional information
-
enzyme is translated as single precursor polypeptide and then processed by proteolytic processing to the active form consisting of two subunits
additional information
-
the large subunit of all recombinant acylases is 55000 Da, the small subunits, 20500 Da, are always larger than that of the native enzyme
additional information
-
the 87000 Da enzyme precursor protein is processed post-translationally at 37°C, 0.1% SDS for 1 h to 60000 Da and 19000 Da peptides by its own proteolytic activity
-
additional information
-
enzyme is translated as single precursor polypeptide and then processed by proteolytic processing to the active form consisting of two subunits
-
additional information
-
the large subunit of all recombinant acylases is 55000 Da, the small subunits, 20500 Da, are always larger than that of the native enzyme
-
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proteolytic modification
-
enzyme is translated as single precursor polypeptide and then processed by proteolytic modification to the active form consisting of two subunits
proteolytic modification
-
aculeacin A acylase partially processed by proteases present in each host strain or by autocatalysis, or other processing enzymes concerned with maturation of the small subunit might exist specifically in Actinoplanes utahensis, because small subunits of all recombinant acylases have a different molecular size from that of native Actinoplanes utahensis
proteolytic modification
-
the 87000 Da enzyme precursor protein is processed post-translationally at 37°C, 0.1% SDS for 1 h to 60000 Da and 19000 Da peptides by its own proteolytic activity
proteolytic modification
-
several steps of post-translational proteolytic modification
proteolytic modification
-
enzyme is synthesized initially as a single polypeptide containing a leader peptide, the small subunit, spacer petides, and the large subunit. The precursor is converted to the active heterodimeric form by post-translational proteolytic modification
proteolytic modification
-
productivity of acylase is effected by proteolytic activity in the host strains of recombinant acylases
proteolytic modification
-
the 87000 Da enzyme precursor protein is processed post-translationally at 37°C, 0.1% SDS for 1 h to 60000 Da and 19000 Da peptides by its own proteolytic activity
-
proteolytic modification
-
enzyme is translated as single precursor polypeptide and then processed by proteolytic modification to the active form consisting of two subunits
-
proteolytic modification
-
aculeacin A acylase partially processed by proteases present in each host strain or by autocatalysis, or other processing enzymes concerned with maturation of the small subunit might exist specifically in Actinoplanes utahensis, because small subunits of all recombinant acylases have a different molecular size from that of native Actinoplanes utahensis
-
proteolytic modification
-
several steps of post-translational proteolytic modification
-
proteolytic modification
-
enzyme is synthesized initially as a single polypeptide containing a leader peptide, the small subunit, spacer petides, and the large subunit. The precursor is converted to the active heterodimeric form by post-translational proteolytic modification
-
proteolytic modification
-
productivity of acylase is effected by proteolytic activity in the host strains of recombinant acylases
-
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biotechnology
-
recombinant enzyme covalently immobilized onto several epoxy-activated supports in order to obtain a robust biocatalyst to be used in industrial bioreactors. The best biocatalyst is obtained by attaching the enzyme on Sepabeads EC-EP5
pharmacology
-
useful in preparing deacylated peptides which are used as starting material for semisynthetic antifungal antibiotics, for creating new and more useful antifungal agents
pharmacology
-
useful in producing peptide nuclei, i.e. deacetylated cyclic hexapeptides, for creating new antifungal agents by introducing different acyl moieties
pharmacology
-
useful in preparing deacylated peptides which are used as starting material for semisynthetic antifungal antibiotics, for creating new and more useful antifungal agents
-
pharmacology
-
useful in producing peptide nuclei, i.e. deacetylated cyclic hexapeptides, for creating new antifungal agents by introducing different acyl moieties
-
synthesis
-
useful in producing peptide nuclei for creating new antifungal agents by introducing different acyl moieties
synthesis
-
useful in preparing deacylated peptides which are used as starting material for semisynthetic antifungal antibiotics. Enzyme is used industrially on a large scale to produce the peptide nuclei , i.e. deacetylated cyclic hexapeptides
synthesis
-
AuAAC should be considered an industrial biocatalyst with high potential in the production of semisynthetic penicillins
synthesis
antibiotic acylases are key enzymes for the industrial production of antibiotic drugs
synthesis
-
antibiotic acylases are key enzymes for the industrial production of antibiotic drugs
-
synthesis
-
useful in preparing deacylated peptides which are used as starting material for semisynthetic antifungal antibiotics. Enzyme is used industrially on a large scale to produce the peptide nuclei , i.e. deacetylated cyclic hexapeptides
-
synthesis
-
useful in producing peptide nuclei for creating new antifungal agents by introducing different acyl moieties
-
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Takeshima, H.; Inokoshi, J.; Takada, Y.; Tanaka, H.; Omura, S.
A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization
J. Biochem.
105
606-610
1989
Actinoplanes utahensis, Actinoplanes utahensis NRRL 12052
brenda
Inokoshi, J.; Takeshima, H.; Omura, S.
Identification of precursor peptide of aculeacin A acylase as a protein with proteolytic activity
FEMS Microbiol. Lett.
114
305-310
1993
Actinoplanes utahensis, Actinoplanes utahensis NRRL 12052
-
brenda
Inokoshi, J.; Takeshima, H.; Ikeda, H.; Omura, S.
Cloning and sequencing of the aculeacin A acylase-encoding gene from Actinoplanes utahensis and expression in Streptomyces lividans
Gene
119
29-35
1992
Actinoplanes utahensis, Actinoplanes utahensis NRRL 12052
brenda
Inokoshi, J.; Takeshima, H.; Ikeda, H.; Omura, S.
Efficient production of aculeacin A acylase in recombinant Streptomyces strains
Appl. Microbiol. Biotechnol.
39
532-536
1993
Actinoplanes utahensis, Actinoplanes utahensis NRRL 12052
-
brenda
Torres-Bacete, J.; Hormigo, D.; Stuart, M.; Arroyo, M.; Torres, P.; Castillon, M.P.; Acebal, C.; Garcia, J.L.; de la Mata, I.
Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis
Appl. Environ. Microbiol.
73
5378-5381
2007
Actinoplanes utahensis
brenda
Hormigo, D.; de la Mata, I.; Acebal, C.; Arroyo, M.
Immobilized aculeacin A acylase from Actinoplanes utahensis: characterization of a novel biocatalyst
Biores. Technol.
101
4261-4268
2010
Actinoplanes utahensis
brenda
Isogai, Y.; Nakayama, K.
Alteration of substrate selection of antibiotic acylase from beta-lactam to echinocandin
Protein Eng.
Des. Sel.
49-56
2015
Actinoplanes utahensis (D9N575), Actinoplanes utahensis NRRL 13244 (D9N575)
brenda