Aculeacin-A deacylase

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In enzymology, an aculeacin-A deacylase (EC 3.5.1.70) is an enzyme that catalyzes the chemical reaction that cleaves the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side chain.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase.

[edit] References

• IUBMB entry for 3.5.1.70
• BRENDA references for 3.5.1.70 (Recommended.)
• PubMed references for 3.5.1.70
• PubMed Central references for 3.5.1.70
• Google Scholar references for 3.5.1.70
• Takeshima H, Inokoshi J, Takada Y, Tanaka H, Omura S (Tokyo). "A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization". J. Biochem.: 606–10. PMID 2760018. 

[edit] External links

The CAS registry number for this enzyme class is 121479-50-3.

• IUBMB entry for 3.5.1.70

• KEGG entry for 3.5.1.70

• BRENDA entry for 3.5.1.70

• NiceZyme view of 3.5.1.70

• EC2PDB: PDB structures for 3.5.1.70

• PRIAM entry for 3.5.1.70

• PUMA2 entry for 3.5.1.70

• IntEnz: Integrated Enzyme entry for 3.5.1.70

• MetaCyc entry for 3.5.1.70

• Atomic-resolution structures of enzymes belonging to this class