Production of d-proline from l-arginine using Pseudomonas aeruginosa |
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| Affiliation: | 1. Dipartimento di Biochimica, Biofisica e Patologia Generale, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Naples, Italy;2. Laboratory of Biochemistry, Centre for Protein Engineering, University of Liège, Liège B-4000, Belgium;1. The Research Foundation for Microbial Diseases of Osaka University, 3-1, Yamada-Oka, Suita, Osaka, Japan;2. Department of Pediatrics, Konan Kosei Hospital, 137 Ohmatsubara, Takaya-cho, Konan, Aichi Japan;3. Department of Clinical Laboratory, Konan Kosei Hospital, 137 Ohmatsubara, Takaya-cho, Konan, Aichi, Japan;4. Kanonji Institute, The Research Foundation for Microbial Diseases of Osaka University, 4-1-70, Seto-cho, Kanonji, Kagawa, Japan;1. School of Medical Sciences (Pharmacology) and Bosch Institute, The University of Sydney, New South Wales 2006, Australia;2. School of Chemistry, The University of Sydney, New South Wales 2006, Australia |
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| Abstract: | Several microorganisms that can use (S)-5-[(amino-iminomethyl) amino]-2-chloropentanoic acid (l-Cl-arginine) as a nitrogen source have been isolated, the most interesting of which is a spontaneous mutant of Pseudomonas aeruginosa PAO1 (DSM 10581). In a fermenter, this unique biocatalyst hydrolysed l-Cl-arginine to (S)-5-amino-2-chloropentanoic acid (l-Cl-ornithine), which spontaneously converted to d-proline with inversion of configuration at an apparent average rate of 0.12 mmol −l h−1 OD−1. The enzyme, for which we suggest the name Cl-arginine amidinohydrolase, was best induced by using the substrate l-Cl-arginine as inducer and l-arginine as nitrogen source. The results presented here describe a new route for the production of d-proline from l-arginine, involving a chemical step and a biocatalytic step followed by a spontaneous chemical cyclisation. |
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