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Literature summary for 3.5.1.70 extracted from

  • 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 (1989), J. Biochem., 105, 606-610.
    View publication on PubMed

Application

Application Comment Organism
pharmacology useful in preparing deacylated peptides which are used as starting material for semisynthetic antifungal antibiotics, for creating new and more useful antifungal agents Actinoplanes utahensis
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 Actinoplanes utahensis

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by EDTA, up to 10 mM, no inhibition by Ca2+, Co2+, Cu2+, Mg2+, Mn2+ or Zn2+ Actinoplanes utahensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic data Actinoplanes utahensis
1.53
-
aculeacin A
-
Actinoplanes utahensis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular exoenzyme Actinoplanes utahensis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
KCl 1 M: 1.47fold activation Actinoplanes utahensis
additional information no significant effect, no activation, by Ca2+, Co2+, Cu2+, Mg2+, Mn2+ or Zn2+ Actinoplanes utahensis
NaCl 1 M: 1.69fold activation Actinoplanes utahensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19000
-
1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits Actinoplanes utahensis
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 Actinoplanes utahensis
55000
-
1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits Actinoplanes utahensis

Organism

Organism UniProt Comment Textmining
Actinoplanes utahensis
-
NRRL 12052
-
Actinoplanes utahensis NRRL 12052
-
NRRL 12052
-

Purification (Commentary)

Purification (Comment) Organism
-
Actinoplanes utahensis

Source Tissue

Source Tissue Comment Organism Textmining
culture filtrate
-
Actinoplanes utahensis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.51
-
-
Actinoplanes utahensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aculeacin A + H2O neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics Actinoplanes utahensis cyclo-hexapeptide + palmitic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
aculeacin A + H2O catalyzes deacylation of aculeacin A Actinoplanes utahensis cyclo-hexapeptide + palmitic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
aculeacin A + H2O neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics Actinoplanes utahensis NRRL 12052 cyclo-hexapeptide + palmitic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
aculeacin A + H2O catalyzes deacylation of aculeacin A Actinoplanes utahensis NRRL 12052 cyclo-hexapeptide + palmitic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
echinocandin A + H2O neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics Actinoplanes utahensis cyclo-hexapeptide + linoleic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
echinocandin A + H2O catalyzes deacylation of echinocandin A Actinoplanes utahensis cyclo-hexapeptide + linoleic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
echinocandin C + H2O neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics Actinoplanes utahensis cyclo-hexapeptide + linoleic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
echinocandin C + H2O catalyzes deacylation of echinocandin C Actinoplanes utahensis cyclo-hexapeptide + linoleic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
echinocandin D + H2O neutral lipopeptide antiyeast, antifungal antibiotic, belongs to echinocandin type antibiotics Actinoplanes utahensis cyclo-hexapeptide + linoleic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
echinocandin D + H2O catalyzes deacylation of echinocandin D Actinoplanes utahensis cyclo-hexapeptide + linoleic acid deacylated peptide, peptide nucleus, has been used as starting compound for creating new and more useful antifungal agents ?
additional information substrate specificity Actinoplanes utahensis ?
-
?
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 Actinoplanes utahensis ?
-
?
additional information no significant activity with ampicillin, tunicamycin, colistin, lankacidin C or blasticidin S Actinoplanes utahensis ?
-
?
additional information substrate specificity Actinoplanes utahensis NRRL 12052 ?
-
?
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 Actinoplanes utahensis NRRL 12052 ?
-
?
additional information no significant activity with ampicillin, tunicamycin, colistin, lankacidin C or blasticidin S Actinoplanes utahensis NRRL 12052 ?
-
?

Subunits

Subunits Comment Organism
dimer 1 * 55000 + 1 * 19000, SDS-PAGE or gel filtration in the presence of 6 M guanidine hydrochloride, two dissimilar subunits Actinoplanes utahensis
dimer two subunits which are associated by a bond other than disulfide bond Actinoplanes utahensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Actinoplanes utahensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
4 h, inactivation at pH 2, stable at pH 4-8 Actinoplanes utahensis
60
-
24 h, 0.1 M phosphate buffer, pH 7, stable at Actinoplanes utahensis
70
-
above, 0.1 M phosphate buffer, pH 7, rapid loss of activity Actinoplanes utahensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pI: above 10.25 Actinoplanes utahensis
7
-
-
Actinoplanes utahensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
2
-
4 h, 30°C: inactivation Actinoplanes utahensis
4 8 4 h, 30°C: stable at Actinoplanes utahensis