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Literature summary for 2.6.1.45 extracted from

  • Modde, K.; Timm, S.; Florian, A.; Michl, K.; Fernie, A.R.; Bauwe, H.
    High serine glyoxylate aminotransferase activity lowers leaf daytime serine levels, inducing the phosphoserine pathway in Arabidopsis (2017), J. Exp. Bot., 68, 643-656 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.45

Cloned(Commentary)

Cloned (Comment) Organism
gene sgat, transgenic overexpression of Flaveria pringlei SGAT in Arabidopsis thaliana ecotype Col-0 rosette leaves via transfection with Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR enzyme expression analysis Flaveria pringlei

Protein Variants

Protein Variants Comment Organism
additional information elevated SGAT activity through transgenic overexpression of Flaveria pringlei SGAT causes clear changes in metabolism and interferes with photosynthetic CO2 uptake and biomass accumulation of Arabidopsis thaliana. The faster serine turnover during photorespiration progressively lowers day-time leaf serine contents and in turn induces the phosphoserine pathway. Transcriptional upregulation of this additional route of serine biosynthesis occurs already during the day but particularly at night, efficiently counteracting night-time serine depletion. Additionally, higher SGAT activity results in an increased use of asparagine as the external donor of amino groups to the photorespiratory pathway but does not alter leaf asparagine content at night. Phenotype, detailed overview Flaveria pringlei
additional information transgenic overexpression of Flaveria pringlei SGAT in Arabidopsis thaliana rosette leaves via transfection with Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR enzyme expression analysis Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
 Flaveria pringlei 5777
-
peroxisome
-
 Arabidopsis thaliana 5777
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine + glyoxylate Flaveria pringlei
-
 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Arabidopsis thaliana
-
 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate Arabidopsis thaliana Col-0
-
 3-hydroxypyruvate + glycine
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q56YA5
-
-
Arabidopsis thaliana Col-0 Q56YA5
-
-
Flaveria pringlei
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + glyoxylate
-
 Flaveria pringlei 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate
-
 Arabidopsis thaliana 3-hydroxypyruvate + glycine
-
 ?
L-serine + glyoxylate
-
 Arabidopsis thaliana Col-0 3-hydroxypyruvate + glycine
-
 ?

Synonyms

Synonyms Comment Organism
FpSGAT
-
 Flaveria pringlei
serine:glyoxylate aminotransferase
-
 Flaveria pringlei
serine:glyoxylate aminotransferase
-
 Arabidopsis thaliana
SGAT
-
 Flaveria pringlei
SGAT
-
 Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP Flaveria pringlei
pyridoxal 5'-phosphate PLP Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction elevated SGAT activity through transgenic overexpression of Flaveria pringlei SGAT causes clear changes in metabolism and interferes with photosynthetic CO2 uptake and biomass accumulation of Arabidopsis. The faster serine turnover during photorespiration progressively lowers day-time leaf serine contents and in turn induces the phosphoserine pathway. Transcriptional upregulation of this additional route of serine biosynthesis occurs already during the day but particularly at night, efficiently counteracting night-time serine depletion. Additionally, higher SGAT activity results in an increased use of asparagine as the external donor of amino groups to the photorespiratory pathway but does not alter leaf asparagine content at night. These results suggest leaf SGAT activity needs to be dynamically adjusted to ensure (i) variable flux through the photorespiratory pathway at a minimal consumption of asparagine and (ii) adequate serine levels for other cellular metabolism, phenotype analysis. Impact of excess SGAT activity on the photorespiratory pathway and photorespiratory nitrogen cycling, schematic overview Arabidopsis thaliana
metabolism serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview Arabidopsis thaliana
physiological function serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate Flaveria pringlei
physiological function serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview Arabidopsis thaliana