| 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
|
| Resource |
| Silkworms |
p50T
b94 |
