Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l ‐serine synthesis from silkworm, Bombyx mori-Reference-Cited by-同舟云学术

Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l ‐serine synthesis from silkworm, Bombyx mori

Published:2019-04-19 Issue:2 Volume:101 Page:e21553
ISSN:0739-4462
Container-title:Archives of Insect Biochemistry and Physiology
language:en
Short-container-title:Arch. Insect Biochem. Physiol

Author:

Haque Mohammad R.¹,Hirowatari Aiko¹,Koyanagi Ayumi¹,Ichinose Takashi¹,Abiru Maiko¹,Mohri Shinya¹,Furuya Shigeki¹,Yamamoto Kohji¹^ORCID

Affiliation:

1. Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental SciencesFaculty of Agriculture, Kyushu UniversityFukuoka Japan

Funder

JSPS KAKENHI

National Bio-Resource Project

Publisher

Wiley

Subject

Insect Science,General Medicine,Biochemistry,Physiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/arch.21553

Reference26 articles.

1. Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways

2. Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of l-serine biosynthesis

3. Phosphoserine Aminotransferase, the Second Step-Catalyzing Enzyme for Serine Biosynthesis

4. Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing

5. GC/MS-based metabolomic studies reveal key roles of glycine in regulating silk synthesis in silkworm, Bombyx mori

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