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Literature summary for 3.5.1.70 extracted from

  • Inokoshi, J.; Takeshima, H.; Ikeda, H.; Omura, S.
    Efficient production of aculeacin A acylase in recombinant Streptomyces strains (1993), Appl. Microbiol. Biotechnol., 39, 532-536.
No PubMed abstract available
Search for more literature for 3.5.1.70

Cloned(Commentary)

Cloned (Comment) Organism
overexpression and overproduction in Streptomyces lividans JT46, Streptomyces albus J1074, Streptomyces ambofaciens ATCC151540, Streptomyces parvulus 2283, Streptomyces avermitilis K139 and Streptomyces griseus ATCC23345, using multi-copy vector pIJ702 Actinoplanes utahensis

Localization

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification enzyme is translated as single precursor polypeptide and then processed by proteolytic modification to the active form consisting of two subunits Actinoplanes utahensis
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 Actinoplanes utahensis
proteolytic modification several steps of post-translational proteolytic modification Actinoplanes utahensis
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 Actinoplanes utahensis
proteolytic modification productivity of acylase is effected by proteolytic activity in the host strains of recombinant acylases Actinoplanes utahensis

Purification (Commentary)

Purification (Comment) Organism
from recombinant strains: Streptomyces lividans JT46, Streptomyces avermitilis K139, Streptomyces albus J1074, Streptomyces ambofaciens ATCC151540, Streptomyces parvulus 2283 and Streptomyces griseus ATCC23345 Actinoplanes utahensis

Source Tissue

Source Tissue Comment Organism Textmining
culture filtrate from recombinant strains: Streptomyces lividans, Streptomyces albus, Streptomyces avermitilis, Streptomyces ambofaciens, Streptomyces parvulus and Streptomyces griseus Actinoplanes utahensis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.5 11.5 from recombinant Streptomyces strains Actinoplanes utahensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aculeacin A + H2O
-
 Actinoplanes utahensis cyclo-hexapeptide + palmitic acid
-
 ?
aculeacin A + H2O
-
 Actinoplanes utahensis NRRL 12052 cyclo-hexapeptide + palmitic acid
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Actinoplanes utahensis
More enzyme is translated as single precursor polypeptide and then processed by proteolytic processing to the active form consisting of two subunits Actinoplanes utahensis
More the large subunit of all recombinant acylases is 55000 Da, the small subunits, 20500 Da, are always larger than that of the native enzyme Actinoplanes utahensis