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This characteristics made this enzyme suitable for structure function studies.
In PlasmoNet, a secondary bypass through agmatinase (EC 3.5.1.53) made this enzyme dispensable.
The unique catalytic characteristics of L. donovani adenosine kinase (LdAdk) and its stage-specific differential activity pattern have made this enzyme a prospective target for chemotherapeutic manipulation in the purine-auxotrophic parasitic protozoan such as L. donovani [ 13].
Consequently, such biological importance and global effects that LpdA is likely to exert on the cellular physiology made this enzyme component an ideal target for the application of FMB.
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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.
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
High stability above pH 6 and resistance to many metal ions make this enzyme suitable for application in wastewater treatment.
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).
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