m6A-dependent mevalonate kinase in juvenile hormone synthesis pathway regulates the diapause process of bivoltine silkworm (Bombyx mori)

Chen, Yanhua; Jiang, Tao; Yasen, Ayinuer; Fan, Bingyan; Zhu, Jianzhong; Wang, Meixian; Qian, Ping; Shen, Xingjia

doi:10.1007/s11033-023-08489-z

Cited by 4 publications

(2 citation statements)

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“…The triphosphate moiety of ATP is mainly fixed by a glycine-rich motif between β6 and α4 (residues 148GAGTGSSA155), as well as residues of Lys11, His213, Asp220, and Thr260. The GXGXGXXX (S/T/A) pattern in the loop between strand β7 and helix α4 is well conserved in the majority of P-loop kinases/NMP kinases and normally represents a conserved ATP-binding motif [ 20 , 21 ]. The γ-phosphoryl group of ATP is located near the substrate Mev and fixed by Lys11 and Asp220, which are the likely catalytic residues of the GHMP family reaction [ 22 ].…”

Section: Resultsmentioning

confidence: 99%

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Structural Characterization and Functional Analysis of Mevalonate Kinase from Tribolium castaneum (Red Flour Beetle)

Zheng,

Yang,

et al. 2024

IJMS

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Mevalonate kinase (MevK) is an important enzyme in the mevalonate pathway that catalyzes the phosphorylation of mevalonate into phosphomevalonate and is involved in juvenile hormone biosynthesis. Herein, we present a structure model of MevK from the red flour beetle Tribolium castaneum (TcMevK), which adopts a compact α/β conformation that can be divided into two parts: an N-terminal domain and a C-terminal domain. A narrow, deep cavity accommodating the substrate and cofactor was observed at the junction between the two domains of TcMevK. Computational simulation combined with site-directed mutagenesis and biochemical analyses allowed us to define the binding mode of TcMevK to cofactors and substrates. Moreover, TcMevK showed optimal enzyme activity at pH 8.0 and an optimal temperature of 40 °C for mevalonate as the substrate. The expression profiles and RNA interference of TcMevK indicated its critical role in controlling juvenile hormone biosynthesis, as well as its participation in the production of other terpenoids in T. castaneum. These findings improve our understanding of the structural and biochemical features of insect Mevk and provide a structural basis for the design of MevK inhibitors.

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Section: Resultsmentioning

confidence: 99%

“…Insect MevKs are predominantly expressed in the corpora allata [ 19 ] and are involved in the mevalonate pathway. In silkworms, knocking down MevK through RNA interference caused females to lay diapause eggs [ 20 ].…”

Section: Introductionmentioning

confidence: 99%