Purification, Characterization and N-Terminal Sequence of Phosphoserine Aminotransferase from the Green Alga Scenedesmus obliquus, Mutant C-2 A′

Stolz, M.; Dörnemann, D.

doi:10.1515/znc-1994-1-211

Cited by 13 publications

(6 citation statements)

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“…The theoretical molecular mass (40,199) is similar to PSATs from Scenedesmus obliquus and Entamoeba histolytica (Ali & Nozaki, ; Stolz & Dornemann, ) but lower than that from sheep brain (Hirsch & Greenberg, ). The deduced amino acid sequences were homologous to PSATs from H. sapiens , A. pernyi, B. circulans, A. thaliana , and E. coli .…”

Section: Discussionmentioning

confidence: 60%

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

Haque

Hirowatari

Koyanagi

et al. 2019

Arch Insect Biochem Physiol

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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 sericindeficient 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. K E Y W O R D S Bombyx mori, phosphoserine aminotransferase, serine, silkworm Arch. Insect Biochem. Physiol. 2019;101:e21553.wileyonlinelibrary.com/journal/arch

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Section: Discussionmentioning

confidence: 60%

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

Haque

Hirowatari

Koyanagi

et al. 2019

Arch Insect Biochem Physiol

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“…Therefore, to determine the missing parameters required to consider the rst two reactions individually, we have studied the properties of PSerAT, the second step-catalyzing enzyme, using bovine liver as mammalian enzyme source. Although PSerAT has been puri ed from various sources such as bacteria (8,9), legume nodules (10), and a green alga (11), little is known about the mammalian enzyme. Some properties were reported many years ago for a preparation isolated from sheep brain (12).…”

Section: Introductionmentioning

confidence: 99%

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

Basurko¹,

Marche²,

Darriet³

et al. 1999

IUBMB: Life

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As a step toward analyzing the serine biosynthetic pathway in mammals, we have studied the properties of phosphoserine aminotransferase, the second step-catalyzing enzyme. The K(m) values for 3-phosphohydroxypyruvate and L-phosphoserine are 5 and 35 microM, respectively, and those for glutamate and alpha-ketoglutarate are 1.2 and 0.8 mM, respectively. The product inhibition studies strengthened the support for a ping-pong mechanism and allowed evaluation of Ki values for the four substrates. The equilibrium constant evaluated from the kinetic parameters is approximately 40. Additionally, some physical properties relative to the bound coenzyme and the secondary structure were investigated. The results are consistent with a structural relationship between the Escherichia coli enzyme and the mammalian enzyme. The mammalian enzyme has specific kinetic parameters, the determination of which is a prerequisite to analyzing the serine biosynthetic pathway in mammals.

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“…In the phosphorylated pathway, the glycolytic intermediate, phosphoglycerate, is oxidized by phosphoglycerate dehydrogenase to form phosphohydroxypyruvate, which in turn is transaminased by phosphoserine aminotransferase to yield phosphoserine. In the final step, dephosphorylation of phosphoserine is catalyzed by phosphoserine phosphatase ( Ichihara & Greenberg 1957;Stolz & Dörnemann 1994). It has been proposed that the latter pathway is probably of minor significance compared to the photorespiratory pathway during daylight hours where photorespiration takes place, but may be of more importance in the dark or early in leaf development ( Ireland & Hiltz 1995).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis fromArabidopsis

Noji

Saito

et al. 1998

The Plant Journal

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SummarySerine biosynthesis in plants proceeds by two pathways; a photorespiratory pathway which is associated with photorespiration and a pathway from phosphoglycerate. A cDNA encoding plastidic phosphoserine aminotransferase (PSAT) which catalyzes the formation of phosphoserine from phosphohydroxypyruvate has been isolated from Arabidopsis thaliana. Genomic DNA blot analysis indicated that this enzyme is most probably encoded by a single gene and is mapped on the lower arm of chromosome 4. The deduced protein contains an N-terminal extension exhibiting the general features of a plastidic transit peptide, which was confirmed by subcellular organelle localization using GFP (green flourescence protein). Northern analysis indicated preferential expression of PSAT in roots of light-grown plants, supporting the idea that the phosphorylated pathway may play an important role in supplying the serine requirement of plants in non-green tissues. In situ hybridization analysis of PSAT revealed that the gene is generally expressed in all types of cells with a significantly higher amount in the meristem tissue of root tips.

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Purification, Characterization and N-Terminal Sequence of Phosphoserine Aminotransferase from the Green Alga Scenedesmus obliquus, Mutant C-2 A′

Cited by 13 publications

References 0 publications

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

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

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

Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis fromArabidopsis

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