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Information on EC 2.6.1.44 - alanine-glyoxylate transaminase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9S7E9
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2.6.1.44 alanine-glyoxylate transaminaseIUBMB Comments
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
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Word Map
- 2.6.1.44
- hyperoxaluria
- peroxisomal
-
end-stage
- oxalosis
- nephrocalcinosis
-
transamination
- dimethylarginine
- stone
- urolithiasis
-
mistargeting
- pyridoxine
- nephrolithiasis
- medicine
-
liver-kidney
- hydroxypyruvate
- grhpr
- analysis
- diagnostics
- nutrition
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
agxt2, alanine-glyoxylate aminotransferase, alanine glyoxylate aminotransferase, spt/agt, alanine-glyoxylate aminotransferase 2, alanine:glyoxylate aminotransferase 1, agt-mi, alanine:2-oxoglutarate aminotransferase, serine pyruvate aminotransferase, cytosolic alanine aminotransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGT
-
-
-
-
alanine-glyoxylate aminotransferase
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-
-
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alanine-glyoxylic aminotransferase
-
-
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alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase
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At3g08860
L-alanine-glycine transaminase
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-
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L-alanine-glyoxylate aminotransferase
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-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:glyoxylate aminotransferase
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
CAS REGISTRY NUMBER
COMMENTARY
9015-67-2
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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 + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
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-
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ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
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-
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ir
L-alanine + glyoxylate
pyruvate + glycine
photorespiratory enzyme
-
ir
additional information
?
-
enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
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-
-
additional information
?
-
-
enzymatic activity is not detected using beta-alanine as the amino donor with either pyruvate or glyoxylate as amino acceptors
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-
-
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-alanine + glyoxylate
pyruvate + glycine
photorespiratory enzyme
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ir
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
L-serine
pH 7.0, 37°C, SGT activity, pyruvate as amino acceptor
1.52
L-serine
pH 7.0, 37°C, SGT activity, glyoxylate as amino acceptor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the first 93 nucleotides of the full-length cDNA are predicted to encode the signal sequence that denote localization to the mitochondria
the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1)
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
aminotransferase enzymes function via a bimolecular double displacement ping-pong mechanism where an amino acid usually serves as the amino donor and an alpha-keto acid serves as the amino acceptor. Aminotransferases are ubiquitous in the three domains of life and are involved in a variety of metabolic pathways including amino acid metabolism, nitrogen assimilation, gluconeogenesis, responses to a number of biotic/abiotic stresses, and among other pathways. The aminotransferase gene family in the model plant Arabidopsis thaliana consists of 44 genes, eight of which are suggested to be alanine aminotransferases. One of the putative alanine aminotransferases genes, At3g08860, is attributed the function of alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase based on the analysis of gene expression networks and homology to other beta-alanine aminotransferases in plants
metabolism
the expression of At3g08860 is highly coordinated with the genes of the uracil degradation pathway leading to the non-proteinogenic amino acid beta-alanine
physiological function
additional information
physiological function
Arabidopsis thaliana alanine:glyoxylate aminotransferase 1 (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
the enzyme produces beta-alanine, which is an osmoprotectant in plants
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
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
additional information
structural analysis and homology modeling of the At3g08860-encoded enzyme
additional information
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structural analysis and homology modeling of the At3g08860-encoded enzyme
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). GGT2_ARATH
481
0
53444
Swiss-Prot
other Location (Reliability: 2)
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus-RIPL mutants auxotrophic for the amino acids L-alanine and beta-alanine
locus At3g08860, DNA and amino acid sequence determination, analysis, and comparisons, recombinant expression of the enzyme lacking the N-terminal signal sequence and functional complementation of two Escherichia coli mutants (panD and HYE032) auxotrophic for the amino acids, L-alanine (proteinogenic) and beta-alanine (non-proteinogenic). The enzyme is not able to complement the Escherichia coli mutant DL39, that harbors a mutation in the tyrosine aminotransferase (tyrB) gene which leads to auxotrophy for L-tyrosine and L-phenylalanine. Recombinant expression of His-tagged enzyme in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is specifically upregulated in response to osmotic stress, but not other stresses (beta-alanine is an osmoprotectant in plants)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liepman, A.H.; Olsen, L.J.
Peroxisomal alanine: glyoxylate aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thaliana
Plant J.
25
487-498
2001
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
Liepman, A.H.; Olsen, L.J.
Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis
Plant Physiol.
131
215-227
2003
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7E9)
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), Arabidopsis thaliana
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