Identification and characterization of a serine racemase in the silkworm Bombyx mori
Identification and characterization of a serine racemase in the silkworm Bombyx mori
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家蚕丝氨酸消旋酶的鉴定和表征
DOI:
10.1093/jb/mvac026
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发表时间:
2022
期刊:
影响因子:
--
通讯作者:
Ito Tomokazu
中科院分区:
文献类型:
--
作者:
Tanaka Yui;Yoshimura Tohru;Hakamata Maho;Saito Chiaki;Sumitani Megumi;Sezutsu Hideki;Hemmi Hisashi;Ito Tomokazu
The pupae of lepidopterans contain high concentrations of endogenousd-serine. In the silkwormBombyx mori,d-serine is negligible during the larval stage but increases markedly during the pupal stage, reaching 50% of the total free serine. However, the physiological function ofd-serine and the enzyme responsible for its production is unknown. Herein, we identified a new type of pyridoxal 5′-phosphate (PLP)-dependent serine racemase (SR) that catalyses the racemization ofl-serine tod-serine inB. mori. This silkworm SR (BmSR) has an N-terminal PLP-binding domain that is homologous to mammalian SR and a C-terminal putative ligand-binding regulatory-like domain (ACT-like domain) that is absent in mammalian SR. Similar to mammalian SRs, BmSR catalyses the racemization and dehydration of both serine isomers. However, BmSR is different from mammalian SRs as evidenced by its insensitivity to Mg2+/Ca2+and Mg-ATP—which are required for activation of mammalian SRs—and highd-serine dehydration activity. At the pupal stage, the SR activity was predominantly detected in the fat body, which was consistent with the timing and localization ofBmSRexpression. The results are an important first step in elucidating the physiological significance ofd-serine in lepidopterans.