Identification and Characterization of a Novel Carboxylesterase Belonging to Family VIII with Promiscuous Acyltransferase Activity Toward Cyanidin-3-O-Glucoside from a Soil Metagenomic Library

Zhang, Yueqi; Ding, Liping; Yan, Zhenzhen; Zhou, Dandan; Jiang, Junwei; Qiu, Jiarong; Xin, Zhihong

doi:10.1007/s12010-021-03614-9

Cited by 5 publications

(2 citation statements)

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“…The engineered EstCE1 had a preference for the larger sugars maltose and maltotriose, compared to EstA that preferentially acylated glucose. Interestingly, the family VIII carboxylesterase EstXT1 has subsequently been shown to acylate cyanidin-3- O -glucoside, suggesting that sugar acylating activities are not rare among the family VIII carboxylesterases …”

Section: Synthetic Applications and Choice Of Acyl Donormentioning

confidence: 99%

“…Interestingly, the family VIII carboxylesterase EstXT1 has subsequently been shown to acylate cyanidin-3-O-glucoside, suggesting that sugar acylating activities are not rare among the family VIII carboxylesterases. 68 ■ CURRENT CHALLENGES AND PROTEIN ENGINEERING Despite the synthetic advantages of promiscuous hydrolases/ acyltransferases in water, the use of lipases in anhydrous solvents is still more common. At the moment this is almost certainly due to the relatively small number of well-studied promiscuous hydrolases/acyltransferases and their synthetic limitations.…”

Section: Hydrolases and Transferasesmentioning

confidence: 99%

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Recent Insights and Future Perspectives on Promiscuous Hydrolases/Acyltransferases

et al. 2021

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Promiscuous hydrolases/acyltransferases have attracted attention for their ability to efficiently catalyze selective transacylation reactions in water to produce esters, thioesters, amides, carbonates, and carbamates. Promiscuous hydrolases/acyltransferases can be implemented into aqueous enzyme cascades and are ideal biocatalysts for the acylation of hydrophilic substrates that are barely soluble in dry organic solvents. This activity was thought to be rare, and recent research has focused on just a small number of accidentally identified promiscuous hydrolases/acyltransferases. High-throughput screening for acyltransferases and an in silico sequence-based method for prediction of acyltransferase activity provided access to many efficient promiscuous hydrolases/acyltransferases, thereby demonstrating that promiscuous acyltransferase activity is rather common in hydrolases. These synthetically valuable enzymes could further be enhanced by protein engineering. This Perspective aims to demonstrate the synthetic potential of these enzymes and raise awareness of the frequency of this activity.

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Section: Synthetic Applications and Choice Of Acyl Donormentioning

confidence: 99%

Section: Hydrolases and Transferasesmentioning

confidence: 99%