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J Biochem. 1989 Apr;105(4):606-10.

A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization.

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Kitasato Institute, Tokyo.


An enzyme, tentatively termed aculeacin A acylase, useful in preparing deacylated peptides which are used as starting material for semisynthetic antifungal antibiotics, was purified from the culture filtrate of Actinoplanes utahensis NRRL12052. The purification involved ultrafiltration and column chromatographies on DEAE-cellulose, hydroxyapatite, and Butyl-Toyopearl 650M. The purified enzyme was composed of two dissimilar subunits with molecular weights of 55,000 and 19,000. The subunits were dissociated in the presence of 0.1% SDS or 6 M guanidine hydrochloride; the dissociation accompanied loss of acylase activity. The enzyme was fully active at pH 7.0 and at 60 degrees C. Its pI was estimated to be above 10.25. The Km and Vmax for aculeacin A were 1.53 mM and 39.7 mumol/min/mg-protein, respectively.

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