Studies on the reaction specificity of the flavoprotein lysine monooxygenase with modified substrates☆
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Cited by (4)
Flavoprotein monooxygenases: Versatile biocatalysts
2021, Biotechnology AdvancesCitation Excerpt :They have been proposed to use enzyme-bound hydrogen peroxide for the monooxygenation of the intermediate product, generated during the reductive half-reaction (Fig. 10) (Lockridge et al., 1972; Ralph et al., 2006). Group G enzymes catalyze oxygenative decarboxylation reactions of several amino acids such as arginine (AMO; EC 1.13.12.1 (van Thoai and Olomucki, 1962a, 1962b)), lysine (LMO; EC 1.13.12.2; Fig. 10a) (Ohnishi et al., 1976)), tryptophan (TMO; EC 1.13.12.3 (Gaweska et al., 2013)) and phenylalanine (PAO; EC 1.13.12.9; Fig. 10b) (Ida et al., 2008)) to give the corresponding amides. Depending on the amino acid used, group G enzymes can also function as oxidases, thereby converting the intermediate imino acids through oxidative deamination to α-keto acids (Fig. 10a and 10b).
Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501
2006, Journal of BiochemistryA novel enzyme, l-tryptophan oxidase, from a basidiomycete, coprinus sp. sf-1: Purification and characterization
2000, Bioscience, Biotechnology and Biochemistryl-Lysine-2-monooxygenase production by strains of Pseudomonas fluorescens and P. putida
1994, World Journal of Microbiology and Biotechnology
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This work has been supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture, Japan, and by a grant from the Tanabe Amino Acid Research Foundation. This is paper IX in a series entitled “Studies on Monooxygenases.” The preceding paper is Ref. (21).
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Present address: Mitsui Petroleum Chemistry Company, Otake, Hiroshima, Japan.