A flavoprotein from the bacterium Streptomyces noursei. The enzyme can also oxidize several other cyclo dipeptides, the best being cyclo(L-tryptophyl-L-tryptophyl) and cyclo(L-phenylalanyl-L-phenylalanyl) [1,2].
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The expected taxonomic range for this enzyme is: Actinobacteria
A flavoprotein from the bacterium Streptomyces noursei. The enzyme can also oxidize several other cyclo dipeptides, the best being cyclo(L-tryptophyl-L-tryptophyl) and cyclo(L-phenylalanyl-L-phenylalanyl) [1,2].
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
albonoursin is then methoxylated to cyclo(L-methoxytyrosine-L-leucine) by O-methyltranferases, encoded by genes B005_4460 and B005_4464, termed albM1 and albM2
albonoursin is then methoxylated to cyclo(L-methoxytyrosine-L-leucine) by O-methyltranferases, encoded by genes B005_4460 and B005_4464, termed albM1 and albM2
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
the catalytic reaction of the natural substrate cyclo(L-leucyl-L-phenylalanyl) occurs in a two-step sequential reaction leading first to cyclo(alpha,beta-dehydro-Phe-L-Leu) and finally to albonoursin
about 50% residual activity in the presence of 1 M NaCl, about 30% residual activity in the presence of 2 M NaCl, about 10% residual activity in the presence of 4 M NaCl, about 3.5% residual activity in the presence of 6 M NaCl
the albABC gene operon deletion mutant of Nocariopsis alba cannot produce cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
the albABC gene operon deletion mutant of Nocariopsis alba cannot produce cyclic dipeptides, cyclo(DELTAPhe-DELTALeu) i.e. albonoursin, and cyclo(DELTAmTyr-DELTALeu)
generation of an albABC gene deletion mutant YL001 of Nocardiopsis alba, genetic organization, overview. Strain YL001 show no significant difference from the wild-type in colonial morphology, and it has a slightly vibrant growth on the MS agar, production of the cyclic dipeptides is abolished in the DELTAalbABC mutant
generation of an albABC gene deletion mutant YL001 of Nocardiopsis alba, genetic organization, overview. Strain YL001 show no significant difference from the wild-type in colonial morphology, and it has a slightly vibrant growth on the MS agar, production of the cyclic dipeptides is abolished in the DELTAalbABC mutant
the enzyme activity is quite stable at neutral and basic pH values, whereas it decreases at acidic pH values. Residual activity is 75% after 6.5 h at pH 6.0
the enzyme is encoded in the albonoursin biosynthetic gene cluster, albABC, genes albAB encode units for a cyclic dipeptide oxidase complex, responsible for generating two dehydrogenated double bonds
Gondry, M.; Lautru, S.; Fusai, G.; Meunier, G.; Menez, A.; Genet, R.
Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl alpha,beta-dehydrogenase
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1.3.3.13 albonoursin synthase
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