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A new bacterial mannosidase for the selective modification of ramoplanin and its derivatives
Institution:1. Istituto di Chimica Organica, Università di Milano, Via Venezian 21, 20133 Milano, Italy;2. ACTYGEA, Via R. Lepetit 34, 21040 Gerenzano (VA), Italy;3. Dipartimento di Biotecnologie e Scienze Molecolari, Università degli Studi dell’Insubria, Via J.H. Dunant 3, 21100 Varese, Italy;4. Dipartimento di Scienze e Tecnologie Alimentari e Microbiologiche, Università di Milano, Via Celoria 2, 20133 Milano, Italy;1. Department of Family Medicine, University of KwaZulu-Natal, Durban, South Africa;2. Third Department of Internal Medicine, University of Fukui Faculty of Medicine Sciences, Fukui, Japan;3. Department of Women’s Health and HIV Research Group, Nelson R Mandela School of Medicine, University of KwaZulu-Natal, Durban, South Africa;4. Department of Family Medicine, School of Nursing and Public Health, University of KwaZulu-Natal, Durban, South Africa;1. Anadolu University, Faculty of Pharmacy, Department of Pharmaceutical Microbiology, 26470 Eski?ehir, Turkey;2. Anadolu University, Faculty of Pharmacy, Department of Pharmaceutical Chemistry, 26470 Eski?ehir, Turkey;3. Anadolu University, Faculty of Pharmacy, Doping and Narcotic Compounds Analysis Laboratory, 26470 Eski?ehir, Turkey;4. Anadolu University, Faculty of Pharmacy, Department of Pharmaceutical Toxicology, 26470 Eski?ehir, Turkey;1. Earth Observation Data Integration & Fusion Research Initiative (EDITORIA), The University of Tokyo, Be505, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8505, Japan;2. Department of Plant Ecology, Forestry and Forest Products Research Institute, Matsunosato 1, Tsukuba, Ibaraki 305-8687, Japan;3. Hokkaido Research Centre, Forestry and Forest Products Research Institute, 7 Hitsujigaoka, Toyohira-ku, Sapporo, Hokkaido, Japan;1. Department of Chemical Engineering, National Institute of Technology, Tiruchirappalli, Tamil Nadu 620015, India;2. Department of Civil Engineering, Anna University Regional Campus, Tirunelveli, Tamil Nadu, India;3. Department of Chemistry, University of Melbourne, Australia;1. Bio-Organic Chemistry Unit, Institute of Biomolecular Chemistry, National Research Council of Italy, Via Campi Flegrei 34, 80078 Pozzuoli, Napoli, Italy;2. Department of Civil and Mechanical Engineering, University of Cassino and Southern Lazio, Via Di Biasio 43, 03043 Cassino, Frosinone, Italy;3. Telematic University Pegaso, Piazza Trieste e Trento 48, 80132 Napoli, Italy;4. UNESCO-IHE Institute for Water Education, Westvest 7, 2611-AX Delft, The Netherlands;1. Department of Chemical Engineering, National Institute of Technology, Tiruchirappalli, Tamil Nadu, 620015, India;2. Department of BioTechnology, KLEF, KL University, Guntur, Andhra Pradesh, 522502, India;3. Department of Life Sciences, Central University of Tamil Nadu, Thiruvarur, Tamil Nadu, 610 005, India;4. Department of Chemistry, University of Melbourne, Australia
Abstract:Ramoplanin is a lipoglycodepsipeptide produced by Actinoplanes sp. ATCC 33076 and active on bacterial cell wall biosynthesis by binding to Lipid II. A screening of an actinomycetes collection was performed to select enzymatic activities able to introduce specific modifications in the ramoplanin molecule. An extracellular mannosidase from Streptomyces GE 91081 was found to selectively remove one mannose unit from ramoplanin and tetrahydroramoplanin to give the corresponding mannosyl aglycones. These molecules show an improved microbiological activity versus some resistant staphylococci and streptococci, and are useful intermediates in the synthesis of novel ramoplanin-like antibiotics. The biotransformation of ramoplanin has been optimised to improve molar conversion and the transformation reaction rate.
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