Molecular survey of the phosphoserine phosphatase involved in L-serine synthesis by silkworms (Bombyx mori).
Insect Mol Biol
; 29(1): 48-55, 2020 02.
Article
de En
| MEDLINE
| ID: mdl-31294881
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.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Sérine
/
Bombyx
/
Phosphoric monoester hydrolases
Limites:
Animals
Langue:
En
Journal:
Insect Mol Biol
Sujet du journal:
BIOLOGIA MOLECULAR
Année:
2020
Type de document:
Article
Pays d'affiliation:
Japon