PMID: 3754135Jan 15, 1986Paper

Purification and characterization of ascamycin-hydrolysing aminopeptidase from Xanthomonas citri

The Biochemical Journal
H Osada, K Isono

Abstract

A nucleoside antibiotic, ascamycin (9-beta-[5'-0-(N-L-alanyl) sulphamoyl-D-ribofuranosyl]-2-chloroadenine), has a selective antibacterial activity against Xanthomonas species. When ascamycin was dealanylated, dealanylascamycin showed a broad antibacterial activity against various Gram-negative and Gram-positive bacteria. Xanthomonas citri is susceptible to ascamycin by virtue of the ascamycin-dealanylating enzyme on the cell surface [Osada & Isono (1985) Antimicrob. Agents Chemother. 27, 230-233]. The enzyme (Xc aminopeptidase) was purified from X. citri cells by successive DEAE-cellulose, chromatofocusing and Sephadex G-100 column chromatography to a homogeneous state. The purified enzyme exhibited a single band with an Mr of 38 000 in SDS/polyacrylamide-gel electrophoresis. Gel filtration on a calibrated column indicated a similar Mr value. The isoelectric point of the enzyme was 5.7. The enzyme catalysed the hydrolysis of the alanyl group of ascamycin and liberated alanine from the sulphamoyl nucleoside. The enzyme also catalysed the hydrolysis of L-proline beta-naphthylamide and L-alanine beta-naphthylamide. The optimal pH and temperature for enzyme activity were pH 7.5-8.0 and 35-40 degrees C respectively. The enzyme was i...Continue Reading

Citations

May 22, 2001·The Journal of Biological Chemistry·T ByunA M Blinkovsky
Mar 17, 2015·The Plant Pathology Journal·Dong Wan Lee, Beom Seok Kim
Sep 27, 2019·The Journal of Antibiotics·Hiroyuki Osada
Jul 1, 1996·FEMS Microbiology Reviews·T Gonzales, J Robert-Baudouy
May 1, 2021·Journal of Industrial Microbiology & Biotechnology·Takayoshi AwakawaIkuro Abe

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