RRC ID 64948
Author Yamamoto K, Mohri S, Furuya S.
Title D-3-phosphoglycerate dehydrogenase from the silkworm Bombyx mori: Identification, functional characterization, and expression.
Journal Arch Insect Biochem Physiol
Abstract 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.
Volume 106(1)
Pages e21751
Published 2021-1-1
DOI 10.1002/arch.21751
PMID 33058282
MeSH Animals Bombyx* / genetics Bombyx* / metabolism Gene Expression Genes, Insect Insect Proteins / metabolism Larva / metabolism Phosphoglycerate Dehydrogenase* / analysis Phosphoglycerate Dehydrogenase* / genetics Phosphoglycerate Dehydrogenase* / metabolism Phylogeny Serine / biosynthesis*
IF 1.536