d-Alanine dehydrogenase |
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Authors: | D Pioli W A Venables F C H Franklin |
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Institution: | (1) Department of Microbiology, University College, Newport Road, CF2 1TA Cardiff, England;(2) Present address: The Corporate Laboratory, Biosciences Group, ICI Ltd., The Heath, WA7 4QE Runcorn, Cheshire, England |
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Abstract: | Pseudomonas aeruginosa PA01 was found to utilise both thed- andl-isomers of -alanine and also -alanine as sole sources of carbon and energy for growth. Enzymological studies of wild-type cultures and comparison with mutants deficient in growth upon one or more isomers of alanine led to the following conclusions: (i) utilisation ofd-alanine involved its direct oxidation by an inducible, membrane-bound, cytochrome-linked dehydrogenase; (ii) utilisation ofl-alanine required its conversion to the directly oxidisabled-form by a soluble racemase; (iii) utilisation of -alanine, likel-alanine, involves both the racemase andd-alanine dehydrogenase enzymes, but in addition must involve other enzymes the identity, of which is still speculative; (iv)P. aeruginosa, likeEscherichia coli, appears to take upd-alanine andl-alanine by means of two specific permeases.Abbreviation DCPIP
2,6-dichlorophenol-indophenol |
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Keywords: | d-Alanine" target="_blank">d-Alanine l-Alanine" target="_blank">l-Alanine -Alanine" target="_blank">gif" alt="beta" align="MIDDLE" BORDER="0">-Alanine Dehydrogenase Oxidase Pseudomonas aeruginosa Catabolism |
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