RRC ID 58987
Author Haque MR, Hirowatari A, Saruta F, Furuya S, Yamamoto K.
Title Molecular survey of the phosphoserine phosphatase involved in L-serine synthesis by silkworms (Bombyx mori).
Journal Insect Mol Biol
Abstract Phosphoserine phosphatase (PSP) catalyses the synthesis of l-serine via the phosphorylated pathway by facilitating the dephosphorylation of phosphoserine. A cDNA encoding PSP from the silkworm Bombyx mori (bmPSP) was isolated using reverse transcription-PCR and then sequenced. The resulting clone encoded 236 amino acids with a molecular weight of 26 150, exhibiting 14-60% sequence identity with other PSPs. The recombinant PSP was overexpressed in Escherichia coli and purified. Kinetic studies showed that bmPSP possessed activity toward l-phosphoserine, and Asp20, Asp22 and Asp204 in bmPSP were found to be critical for modulating bmPSP activity. Real-time PCR analysis provided evidence that the amount of bmpsp transcript was reduced in middle silk glands of a sericin-deficient silkworm strain. These findings revealed that bmPSP may play important roles in synthesizing one-carbon donors of l-serine, which is abundant in silk, as well as other cell metabolites in B. mori.
Volume 29(1)
Pages 48-55
Published 2020-2-1
DOI 10.1111/imb.12609
PMID 31294881
MeSH Amino Acid Sequence Animals Bombyx / enzymology* Bombyx / genetics Bombyx / metabolism Cloning, Molecular DNA, Complementary / genetics Escherichia coli Insect Proteins / biosynthesis Insect Proteins / metabolism Larva / metabolism Phosphoric Monoester Hydrolases / chemistry* Phosphoric Monoester Hydrolases / genetics Phosphoric Monoester Hydrolases / metabolism Serine / biosynthesis* Silk
IF 2.533
Times Cited 0
Silkworms p50T b94