TY - JOUR
T1 - D-3-phosphoglycerate dehydrogenase from the silkworm Bombyx mori
T2 - Identification, functional characterization, and expression
AU - Yamamoto, Kohji
AU - Mohri, Shinya
AU - Furuya, Shigeki
N1 - Funding Information:
This study was supported by a Grant‐in‐Aid for Scientific Research (KAKENHI, 17K19272, and 16KK0172) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. The work was also supported in part by the Research Grant for Young Investigators of Faculty of Agriculture, Kyushu University.
PY - 2021/1
Y1 - 2021/1
N2 - 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.
AB - 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.
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U2 - 10.1002/arch.21751
DO - 10.1002/arch.21751
M3 - Article
AN - SCOPUS:85092478771
VL - 106
JO - Archives of Insect Biochemistry and Physiology
JF - Archives of Insect Biochemistry and Physiology
SN - 0739-4462
IS - 1
M1 - e21751
ER -