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Literature summary extracted from
- Alteration of substrate selection of antibiotic acylase from beta-lactam to echinocandin (2015), Protein Eng., Des. Sel., 49-56 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.5.1.70 | synthesis | antibiotic acylases are key enzymes for the industrial production of antibiotic drugs | Actinoplanes utahensis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.70 | gene aac1, DNA and amino acid sequence determination and analysis | Actinoplanes utahensis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.70 | aculeacin A + H2O | Actinoplanes utahensis | - |
cyclo-hexapeptide + palmitic acid | - |
? |  |
| 3.5.1.70 | aculeacin A + H2O | Actinoplanes utahensis NRRL 13244 | - |
cyclo-hexapeptide + palmitic acid | - |
? | |
| 3.5.1.70 | echinocandin A + H2O | Actinoplanes utahensis | - |
cyclo-hexapeptide + linoleic acid | - |
? | |
| 3.5.1.70 | echinocandin A + H2O | Actinoplanes utahensis NRRL 13244 | - |
cyclo-hexapeptide + linoleic acid | - |
? | |
| 3.5.1.70 | additional information | Actinoplanes utahensis | 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 | ? | - |
? | |
| 3.5.1.70 | 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 | ? | - |
? | |
| 3.5.1.70 | penicillin G + H2O | Actinoplanes utahensis | - |
? | - |
? | |
| 3.5.1.70 | penicillin G + H2O | Actinoplanes utahensis NRRL 13244 | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.70 | Actinoplanes utahensis | D9N575 | - |
- |
| 3.5.1.70 | Actinoplanes utahensis NRRL 13244 | D9N575 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.70 | aculeacin A + H2O | - |
Actinoplanes utahensis | cyclo-hexapeptide + palmitic acid | - |
? | |
| 3.5.1.70 | aculeacin A + H2O | preferred substrate | Actinoplanes utahensis | cyclo-hexapeptide + palmitic acid | - |
? | |
| 3.5.1.70 | aculeacin A + H2O | - |
Actinoplanes utahensis NRRL 13244 | cyclo-hexapeptide + palmitic acid | - |
? | |
| 3.5.1.70 | aculeacin A + H2O | preferred substrate | Actinoplanes utahensis NRRL 13244 | cyclo-hexapeptide + palmitic acid | - |
? | |
| 3.5.1.70 | echinocandin A + H2O | - |
Actinoplanes utahensis | cyclo-hexapeptide + linoleic acid | - |
? | |
| 3.5.1.70 | echinocandin A + H2O | - |
Actinoplanes utahensis NRRL 13244 | cyclo-hexapeptide + linoleic acid | - |
? | |
| 3.5.1.70 | 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 | Actinoplanes utahensis | ? | - |
? | |
| 3.5.1.70 | 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 | Actinoplanes utahensis NRRL 13244 | ? | - |
? | |
| 3.5.1.70 | penicillin G + H2O | - |
Actinoplanes utahensis | ? | - |
? | |
| 3.5.1.70 | penicillin G + H2O | - |
Actinoplanes utahensis NRRL 13244 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.70 | AAC | - |
Actinoplanes utahensis |
| 3.5.1.70 | aac1 | - |
Actinoplanes utahensis |
| 3.5.1.70 | aculeacin A acylase | - |
Actinoplanes utahensis |
| 3.5.1.70 | cyclic lipopeptide acylase | - |
Actinoplanes utahensis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.70 | evolution | the antibiotic acylases belong to the N-terminal nucleophile hydrolase superfamily | Actinoplanes utahensis |
| 3.5.1.70 | 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 | Actinoplanes utahensis |
| 3.5.1.70 | 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 | Actinoplanes utahensis |
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Release 2023.1 (January 2023)
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