In vitro screening for inhibitor of cloned Drosophila melanogaster tyramine-β-hydroxylase and docking studies

Hasan, Md. Nazmul; Thakur, Prasoon Kumar; Abir, Ruhshan Ahmed; Zubaer, Abdullah; Guo, Ruiyun; Yoshida, Mayumi; Ohta, Hiroto; Lee, Jae Man; Kusakabe, Takahiro; Hirashima, Akinori

doi:10.1016/j.ijbiomac.2016.06.026

Cited by 3 publications

(2 citation statements)

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“…Kobayashi and co-workers expressed human DβH in transgenic mice and Gibson and co-workers were able to express DβH in Drosophila melanogaster Schneider 2 (S2) cells . The insect homologue tyramine β-hydroxylase TBM was also expressed in Schneider 2 (S2) cells and a Bombyx mori strain. , Recombinant human DβH expressed in yeast or E. coli can be purchased from different biotechnological companies, such as FisherScientific, Cusabio, or LSBio.…”

Section: Copper-dependent Enzymesmentioning

confidence: 99%

“…97 The insect homologue tyramine β-hydroxylase TBM was also expressed in Schneider 2 (S2) cells and a Bombyx mori strain. 62,98 Recombinant human DβH expressed in yeast or E. coli can be purchased from different biotechnological companies, such as FisherScientific, Cusabio, or LSBio. The crystal structure of DβH was reported in 2016, which presents a crucial step for further research.…”

Section: ■ Metal-free Enzymesmentioning

confidence: 99%

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Enzymatic Hydroxylations of sp³-Carbons

et al. 2021

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Enzymatic hydroxylation of activated and nonactivated sp 3 -carbons attracts keen interest from the chemistry community as it is one of the most challenging tasks in organic synthesis. Nature provides a vast number of enzymes with an enormous catalytic versatility to fulfill this task. Given that those very different enzymes have a distinct specificity in substrate scope, selectivity, activity, stability, and catalytic cycle, it is interesting to outline similarities and differences. In this Review, we intend to delineate which enzymes possess considerable advantages within specific issues. Heterologous production, crystal structure availability, enzyme engineering potential, and substrate promiscuity are essential factors for the applicability of these biocatalysts.

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