Transaminase and D-Amino Acid Oxidase of Trigonopsis variabilis

Abstract

SUhIitIARYThe yeast Trigonopsis variabilis can utilize many single amino acids as sole source of nitrogen. Of the amino acids utilized, the D-isomers are oxidatively deaminated, whilst the L-isomers are transaminated with either a-ketoglutarate or pyruvate. The D-amino acid oxidase activity of this organism, when grown on DL-methionhe as sole source of nitrogen, is the highest yet recorded, and may be rccommended for the preparation of keto acids.

Transcriptional and bioinformatic analysis of the 56.8kb DNA region amplified in tandem repeats containing the penicillin gene cluster in Penicillium chrysogenum

“…An interesting gene present downstream of the penDE is ORF11, encoding a hypothetical protein with a D-amino acid oxidase (deaminating) domain. D-amino oxidases of yeasts and fungi (e.g., Trigonopsis variabilis) are known to convert the D--aminoadipic chain of cephalosporin C or penicillin N to -ketoglutarate (Sentheshanmuganathan and Nicherson, 1962;Pollegioni et al, 2004). -Lactam by-products containing -ketoglutarate instead of -aminoadipate have been reported in -lactam producer strains (Kitano et al, 1976a,b), e.g., the formation of 6-(5-hydroxy-n-valeramido)-penicillanic acid, a product of the deaminating decarboxylation of penicillin N (presumably formed by a D-amino acid oxidase), along with penicillin N was reported in the cephalosporin producer Paecilomyces carneus (Kitano et al, 1976a).…”

D-amino acid oxidase: structure, catalytic mechanism, and practical application

“…show the presence of bacterial DAAO. Currently the enzyme is known to be present in mollusk, fish, reptile, amphibia, insects, birds, mammals (kidney, lungs, brain) [27], and different microorganisms: alga Chlorella vulgaris [28], fungi Neurospora crassa [29], Cephalosporium acre monium [30], Fusarium solani (Nectria haematococca) [31], yeast T. variabilis [32,33], Candida tropicalis [34], R. gracilis (alternate name Rhodosporidium toruloides) [35], Candida boidinii [36], bacteria Streptomyces avermi tilis [24,37], Arthrobacter protophormiae [GenBank accession AY306197], Mycobacterium tuberculosis [23], Agrobacterium tumefaciens C58 [38], etc.…”

Induction of the d-Amino Acid Oxidase from Trigonopsis variabilis

“…Reoxidation of reduced flavin adenine dinucleotide, which is bound tightly to the biocatalyst, occurs by reduction of molecular oxygen, and hydrogen peroxide is released. D-AOs are widely distributed in nature; for example, they occur in vertebrates, especially mammals (8,17,18), and in microorganisms, such as the fungi Cephalosporium acremonium (1), Neurospora crassa (32), Fusarium solani (15), and Fusarium oxysporum (9), the alga Chlorella vulgaris (28), the yeasts Candida tropicalis (37), Trigonopsis variabilis (30), and Rhodotorula gracilis (33), and the bacterium Alcaligenes denitrificans (9).…”