RRC ID 57020
Author Haque MR, Hirowatari A, Koyanagi A, Ichinose T, Abiru M, Mohri S, Furuya S, Yamamoto K.
Title Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l-serine synthesis from silkworm, Bombyx mori.
Journal Arch. Insect Biochem. Physiol.
Abstract In this study, we identified and characterized a phosphoserine aminotransferase (bmPSAT) from Bombyx mori (B. mori) that is responsible for l-serine biosynthesis. A complementary DNA that encodes bmPSAT was cloned by reverse transcriptase polymerase reaction and sequenced. The presumed amino acid sequence revealed 47-87% identity with known PSATs from insects, humans, plants, and bacteria. Through phylogenetic analysis, we found that bmPSAT is evolutionary related to insect PSATs. Recombinant bmPSAT was produced in Escherichia coli by using a cold-shock promotor and purified to homogeneity. This enzyme utilizes phosphohydroxypyruvate and glutamate for transamination. bmPSAT messenger RNA (mRNA) was expressed at higher levels in several tissues of standard strain silkworm including the silk gland, whereas a sericin-deficient silkworm strain exhibited a diminished expression of bmPSAT mRNA in the silk gland. These findings indicate that bmPSAT may play an important role in synthesizing and supplying l-serine in the larva of B. mori.
Volume 101(2)
Pages e21553
Published 2019-6
DOI 10.1002/arch.21553
PMID 31004387
MeSH Animals Bombyx / enzymology* Bombyx / genetics Bombyx / metabolism Cloning, Molecular DNA, Complementary / genetics Escherichia coli / genetics Gene Expression Regulation, Developmental Insect Proteins / biosynthesis Insect Proteins / metabolism Larva / metabolism Phylogeny Recombinant Proteins / metabolism Serine / biosynthesis* Transaminases / chemistry* Transaminases / genetics Transaminases / metabolism
IF 1.316
Resource
Silkworms p50T b94