3.5.1.70: aculeacin-A deacylase
This is an abbreviated version!
For detailed information about aculeacin-A deacylase, go to the full flat file.
Word Map on EC 3.5.1.70
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3.5.1.70
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utahensis
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actinoplanes
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penicillin
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deacylation
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lividans
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aac
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n-acylhomoserine
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synthesis
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lactone
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amide
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homoserine
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quorum
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ralstonia
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heterodimeric
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ahl-acylase
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palmitoyl
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cephalosporin
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oligodeoxyribonucleotide
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beta-lactam
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actinomycete
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elastase
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pharmacology
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echinocandins
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acylases
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quorum-quenching
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quorum-sensing
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cosmid
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biotechnology
- 3.5.1.70
- utahensis
-
actinoplanes
- penicillin
-
deacylation
- lividans
- aac
-
n-acylhomoserine
- synthesis
- lactone
- amide
- homoserine
-
quorum
- ralstonia
-
heterodimeric
- ahl-acylase
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palmitoyl
- cephalosporin
- oligodeoxyribonucleotide
- beta-lactam
-
actinomycete
- elastase
- pharmacology
-
echinocandins
- acylases
-
quorum-quenching
-
quorum-sensing
-
cosmid
- biotechnology
Reaction
Synonyms
AAC, aac1, aculeacin A acylase, AuAAC, cyclic lipopeptide acylase, deacylase, aculeacin A
ECTree
3.5.1.70 aculeacin-A deacylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.70 - aculeacin-A deacylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
penicillin dihydroF + H2O
6-aminopenicillanic acid + hexanoic acid
-
-
-
-
?
penicillin F + H2O
6-aminopenicillanic acid + (3E)-hex-3-enoic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic 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
Actinoplanes utahensis NRRL 13244
preferred substrate
-
-
?
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 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
?
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
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-
?
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
?
-
-
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
?
-
Actinoplanes utahensis NRRL 13244
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
-
-
?
