Matches in SemOpenAlex for { <https://semopenalex.org/work/W2897614183> ?p ?o ?g. }
- W2897614183 endingPage "96" @default.
- W2897614183 startingPage "87" @default.
- W2897614183 abstract "The oxidation of d-amino acids is relevant to neurodegenerative diseases, detoxification, and nutrition in microorganisms and mammals. It is also important for the resolution of racemic amino acid mixtures and the preparation of chiral building blocks for the pharmaceutical and food industry. Considerable biochemical and structural knowledge has been accrued in recent years on the enzymes that carry out the oxidation of the Cα-N bond of d-amino acids. These enzymes contain FAD as a required coenzyme, share similar overall three-dimensional folds and highly conserved active sites, but differ in their specificity for substrates with neutral, anionic, or cationic side-chains. Here, we summarize the current biochemical and structural knowledge regarding substrate specificity on d-amino acid oxidase, d-aspartate oxidase, and d-arginine dehydrogenase for which a wealth of biochemical and structural studies is available." @default.
- W2897614183 created "2018-10-26" @default.
- W2897614183 creator A5023523841 @default.
- W2897614183 creator A5032766595 @default.
- W2897614183 creator A5062065917 @default.
- W2897614183 date "2018-12-01" @default.
- W2897614183 modified "2023-09-24" @default.
- W2897614183 title "Structural determinants for substrate specificity of flavoenzymes oxidizing d-amino acids" @default.
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