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D‐3‐phosphoglycerate dehydrogenase from the silkworm Bombyx mori: Identification, functional characterization, and expression
Archives of Insect Biochemistry and Physiology ( IF 2.2 ) Pub Date : 2020-10-14 , DOI: 10.1002/arch.21751
Kohji Yamamoto 1 , Shinya Mohri 1 , Shigeki Furuya 1
Affiliation  

D‐3‐phosphoglycerate dehydrogenase (PHGDH) is a key enzyme involved in the synthesis of l‐serine. Despite the high serine content in silk proteins and the crucial role of PHGDH in serine biosynthesis, PHGDH has not been described in silkworms to date. Here, we identified PHGDH in the silkworm Bombyx mori and evaluated its biochemical properties. On the basis of the amino acid sequence and phylogenetic tree, this PHGDH has been categorized as a new type and designated as bmPHGDH. The recombinant bmPHGDH was overexpressed and purified to homogeneity. Kinetic studies revealed that PHGDH uses NADH as a coenzyme to reduce phosphohydroxypyruvate. High expression levels of bmphgdh messenger RNA (mRNA) were observed in the middle part of the silk gland and midgut in a standard strain of silkworm. Moreover, a sericin‐deficient silkworm strain displayed reduced expression of bmphgdh mRNA. These findings indicate that bmPHGDH might play a crucial role in the provision of l‐serine in the larva of B. mori.

中文翻译:

家蚕D-3-磷酸甘油酸脱氢酶的鉴定,功能表征和表达

d-3 -磷酸甘油酸脱氢酶(PHGDH)是参与的合成中的关键酶-丝氨酸。尽管丝蛋白中的丝氨酸含量很高,PHGDH在丝氨酸生物合成中起着关键作用,但迄今为止,PHGDH尚未在蚕中得到描述。在这里,我们在家蚕中鉴定了PHGDH并评估了其生化特性。根据氨基酸序列和系统发育树,该PHGDH已被归类为新型,并被命名为bmPHGDH。重组bmPHGDH被过表达并纯化至同质。动力学研究表明,PHGDH使用NADH作为辅酶来还原磷酸羟基丙酮酸。bmphgdh高表达水平在蚕的标准品系的丝腺和中肠中部观察到信使RNA(mRNA)。此外,缺乏丝胶蛋白的家蚕菌株显示bmphgdh mRNA的表达降低。这些结果表明,bmPHGDH可能在提供了至关重要的作用中的幼虫-丝氨酸家蚕
更新日期:2020-10-14
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