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We discovered that my son inherited two different (thus-far-unique) mutations in the same gene — the NGLY1 gene — which encodes the enzyme N-glycanase 1. Consequently, he cannot make this enzyme.
These features, in combination with the biocatalytic properties of BVMOAf1, make this enzyme a promising biocatalyst.
In particular, its wide substrate scope and high stability make this enzyme a potential candidate for various Baeyer-Villiger oxidations.
High stability above pH 6 and resistance to many metal ions make this enzyme suitable for application in wastewater treatment.
These properties make this enzyme to be highly thermostable and may be suggested as a potential candidate for application in some industrial processes.
These features make this enzyme an effective activator of a pro-drug an apro-drug anthapplication acthatly pursued for a variety of thasapeutic strategies.
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This characteristics made this enzyme suitable for structure function studies.
It retained 44% of its maximum activity at 10°C, making this enzyme more attractive for municipal wastewater treatment 10-25°C 10-25°C
The involvement of DDAH function in the regulation of NOS makes this enzyme a potentially attractive therapeutic target.
Furthermore the hydrolysis of dihydrouracils was discovered, making this enzyme a potential tool toward enantiopure β-amino acids applying a modified hydantoinase process (Engel et al. 2012b).
The aldo-keto reductase 1C3 isoform (AKR1C3) plays a vital role in the biosynthesis of androgens, making this enzyme an attractive target for castration-resistant prostate cancer therapy.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com