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Information on EC 2.6.1.45 - serine-glyoxylate transaminase and Organism(s) Arabidopsis thaliana and UniProt Accession Q56YA5
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2.6.1.45 serine-glyoxylate transaminaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 2.6.1.45
- hyperoxaluria
- peroxisomal
- oxalate
- pyridoxal
- hydroxypyruvate
-
liver-specific
-
mistargeting
- pyridoxine
-
photorespiration
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photorespiratory
- oxalosis
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2.6.1.44
-
glutamate:glyoxylate
- hyphomicrobium
- urolithiasis
- nephrocalcinosis
- methylovorum
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peroxisome-to-mitochondrion
-
intraperoxisomal
-
liver-kidney
-
anlage
-
plp-dependent
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alanine:glyoxylate aminotransferase, sgat, serine-glyoxylate aminotransferase, serine:glyoxylate aminotransferase, serine-glyoxylate transaminase, l-serine:glyoxylate aminotransferase, l-serine glyoxylate aminotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, serine-glyoxylate
-
-
-
-
L-serine glyoxylate aminotransferase
-
-
-
-
serine-glyoxylate aminotransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-serine:glyoxylate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
37259-57-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine + 3-hydroxypyruvate
3-hydroxypyruvate + L-serine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
55% of the activity with L-serine and glyoxylate
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine + 3-hydroxypyruvate
3-hydroxypyruvate + L-serine
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
PLP, is bound at the active site but is not held in place by covalent interactions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Aminooxyacetate
reacts with the carbonyl group of pyridoxal phosphate, 88% inhibition at 0.01 mM
beta-chloro-L-alanine
reacts with the carbonyl group of pyridoxal phosphate. 53.9% inhibition at 1 mM
p-hydroxymercuribenzoate
the 24.1% decrease in enzyme activity achieved using 1.0 mM inhibitor might be considered to be unspecific
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1)
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
physiological function
additional information
in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1. Residues Tyr35' and Arg36', entering the active site from the other subunits in the dimer, mediate interactions between AGT and L-serine when used as a substrate. Structural model of AGT1 and structure-function analysis, structure comparisons, detailed overview
physiological function
overexpression in Lemna minor results in increased enzymic activity and decreased endogenous serine levels under salt stress, leading to enhanced protection against root abscission, higher maximum quantum yield of photosystem II, increased defense from cell damage as a result of improved cell membrane integrity, a decrease of reactive oxygen species accumulation, and a strengthened antioxidant system
physiological function
Arabidopsis thaliana serine:glyoxylate aminotransferase (AGT1) is a multifunctional class IV aminotransferase protein that catalyzes transamination reactions using L-serine, L-alanine, and L-asparagine as amino donors and glyoxylate, pyruvate, and hydroxypyruvate as amino acceptors. AGT1 is a peroxisomal aminotransferase with a central role in photorespiration. This enzyme catalyzes various aminotransferase reactions, including serine:glyoxylate, alanine:glyoxylate, and asparagine:glyoxylate transaminations
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SGAT_ARATH
401
0
44208
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1
dimer
crystal structure, enzyme in solution, catalytic enzyme form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in apoform and complexed with L-serine, large, greenish-yellow crystals grow from drops containing equal volumes of 11 mg/ml protein in 0.2 mM PLP, 10% glycerol, and 100 mM Tris-HCl, pH 8.5, and precipitant solution containing 4.1-4.2 M sodium formate, equilibration against the same precipitant, several days, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.1 A resolution, respectively, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P251L
the sat mutation likely affects the dimer interface near the catalytic site, phenotype overview. The point mutation renders the sat mutant plants lethally stunted when grown in normal atmospheric conditions
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
In the roots of 10-day-old seedlings treated for 2 h with 20 mM Asn, the transcript levels are raised by 2fold. During this treatment, the concentration of Asn in root is raised by ca. 5fold
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
overexpression in Lemna minor results in increased enzymic activity and decreased endogenous serine levels under salt stress, leading to enhanced protection against root abscission, higher maximum quantum yield of photosystem II, increased defense from cell damage as a result of improved cell membrane integrity, a decrease of reactive oxygen species accumulation, and a strengthened antioxidant system
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kendziorek, M.; Paszkowski, A.
Properties of serine:glyoxylate aminotransferase purified from Arabidopsis thaliana leaves
Acta Biochim. Biophys. Sin. (Shanghai)
40
102-110
2008
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
Zhang, Q.; Lee, J.; Pandurangan, S.; Clarke, M.; Pajak, A.; Marsolais, F.
Characterization of Arabidopsis serine:glyoxylate aminotransferase, AGT1, as an asparagine aminotransferase
Phytochemistry
85
30-35
2013
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
Yang, L.; Han, H.; Liu, M.; Zuo, Z.; Zhou, K.; L, J.; Zhu, Y.; Bai, Y.; Wang, Y.
Overexpression of the Arabidopsis photorespiratory pathway gene, serine: glyoxylate aminotransferase (AtAGT1), leads to salt stress tolerance in transgenic duckweed (Lemna minor)
Plant Cell Tissue Organ Cult.
113
407-416
2013
Arabidopsis thaliana (Q56YA5)
-
Liepman, A.H.; Vijayalakshmi, J.; Peisach, D.; Hulsebus, B.; Olsen, L.J.; Saper, M.A.
Crystal structure Of photorespiratory alanine glyoxylate aminotransferase 1 (AGT1) from Arabidopsis thaliana
Front. Plant Sci.
10
1229
2019
Arabidopsis thaliana (Q56YA5)
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
J. Exp. Bot.
68
643-656
2017
Flaveria pringlei, Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana Col-0 (Q56YA5)
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