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
-
aac
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n-acylhomoserine
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synthesis
-
lactone
-
amide
-
homoserine
-
quorum
-
ralstonia
-
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
-
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
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Posttranslational Modification
Posttranslational Modification on EC 3.5.1.70 - aculeacin-A deacylase
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proteolytic modification
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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
-