Structural and mechanistic investigations on C C bond forming α-oxoamine synthase allowing L-glutamate as substrate

Zhang, Dai-Ke; Song, Kai-Yuan; Yan, Ya-Qian; Zheng, Jian-Ting; Xu, Jun; Da, Lin-Tai; Xu, Min-Juan

doi:10.1016/j.ijbiomac.2024.131696

International Journal of Biological Macromolecules

2024

DOI: 10.1016/j.ijbiomac.2024.131696

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Structural and mechanistic investigations on C C bond forming α-oxoamine synthase allowing L-glutamate as substrate

Dai-Ke Zhang,

Kai-Yuan Song,

Ya-Qian Yan

et al.

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Rational Engineering of a Thermostable α-Oxoamine Synthase Biocatalyst Expands the Substrate Scope and Synthetic Applicability

Campopiano,

Ashley,

Zhu

et al. 2024

Preprint

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Carbon-carbon bond formation is one of the key pillars of organic synthesis. Green, selective and efficient biocatalytic methods for such are therefore highly desirable. The α-oxoamine synthases (AOSes) are a class of pyridoxal 5’-phosphate (PLP)-dependent, irreversible, carbon-carbon bond-forming enzymes, which have been limited previously by their narrow substrate specificity and requirement of acyl-CoA thioester substrates. We recently characterized a thermophilic enzyme from Thermus thermophilus (ThAOS) with a much broader substrate scope and described its use in a chemo-biocatalytic cascade process to generate pyrroles in good yields and timescales. Herein, we report the structure-guided engineering of ThAOS to arrive at variants able to use a greatly expanded range of amino acid and simplified N-acetylcysteamine (SNAc) acyl-thioester substrates. The crystal structure of the improved ThAOS V79A mutant with a bound PLP:penicillamine external aldimine ligand, provides insight into the properties of the engineered biocatalyst.

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Rational Engineering of a Thermostable α-Oxoamine Synthase Biocatalyst Expands the Substrate Scope and Synthetic Applicability

Campopiano,

Ashley,

Zhu

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

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Structural and mechanistic investigations on C C bond forming α-oxoamine synthase allowing L-glutamate as substrate

Cited by 1 publication

References 61 publications

Rational Engineering of a Thermostable α-Oxoamine Synthase Biocatalyst Expands the Substrate Scope and Synthetic Applicability

Rational Engineering of a Thermostable α-Oxoamine Synthase Biocatalyst Expands the Substrate Scope and Synthetic Applicability

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