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Literature summary extracted from

  • 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 (2019), Front. Plant Sci., 10, 1229 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.14 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 Arabidopsis thaliana
2.6.1.44 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 Arabidopsis thaliana
2.6.1.45 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 Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.14 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 Arabidopsis thaliana
2.6.1.44 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 Arabidopsis thaliana
2.6.1.45 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 Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.14 peroxisome the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1) Arabidopsis thaliana 5777
-
2.6.1.44 peroxisome the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1) Arabidopsis thaliana 5777
-
2.6.1.45 peroxisome the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1) Arabidopsis thaliana 5777
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.14 L-asparagine + 3-hydroxypyruvate Arabidopsis thaliana
-
 2-oxosuccinamate + L-serine
-
 ?
2.6.1.14 L-asparagine + glyoxylate Arabidopsis thaliana
-
 2-oxosuccinamate + glycine
-
 ?
2.6.1.14 L-asparagine + pyruvate Arabidopsis thaliana
-
 2-oxosuccinamate + L-alanine
-
 ?
2.6.1.44 L-alanine + 3-hydroxypyruvate Arabidopsis thaliana
-
 pyruvate + L-serine
-
 ?
2.6.1.44 L-alanine + glyoxylate Arabidopsis thaliana
-
 pyruvate + glycine
-
 ?
2.6.1.44 L-alanine + pyruvate Arabidopsis thaliana
-
 pyruvate + L-alanine
-
 ?
2.6.1.45 L-serine + 3-hydroxypyruvate Arabidopsis thaliana
-
 3-hydroxypyruvate + L-serine
-
 ?
2.6.1.45 L-serine + glyoxylate Arabidopsis thaliana
-
 3-hydroxypyruvate + glycine
-
 ?
2.6.1.45 L-serine + pyruvate Arabidopsis thaliana
-
 3-hydroxypyruvate + L-alanine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.14 Arabidopsis thaliana Q56YA5
-
-
2.6.1.44 Arabidopsis thaliana Q56YA5
-
-
2.6.1.45 Arabidopsis thaliana Q56YA5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.14 L-asparagine + 3-hydroxypyruvate
-
 Arabidopsis thaliana 2-oxosuccinamate + L-serine
-
 ?
2.6.1.14 L-asparagine + glyoxylate
-
 Arabidopsis thaliana 2-oxosuccinamate + glycine
-
 ?
2.6.1.14 L-asparagine + pyruvate
-
 Arabidopsis thaliana 2-oxosuccinamate + L-alanine
-
 ?
2.6.1.44 L-alanine + 3-hydroxypyruvate
-
 Arabidopsis thaliana pyruvate + L-serine
-
 ?
2.6.1.44 L-alanine + glyoxylate
-
 Arabidopsis thaliana pyruvate + glycine
-
 ?
2.6.1.44 L-alanine + pyruvate
-
 Arabidopsis thaliana pyruvate + L-alanine
-
 ?
2.6.1.45 L-serine + 3-hydroxypyruvate
-
 Arabidopsis thaliana 3-hydroxypyruvate + L-serine
-
 ?
2.6.1.45 L-serine + glyoxylate
-
 Arabidopsis thaliana 3-hydroxypyruvate + glycine
-
 ?
2.6.1.45 L-serine + pyruvate
-
 Arabidopsis thaliana 3-hydroxypyruvate + L-alanine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.14 dimer crystal structure, enzyme in solution, catalytic enzyme form Arabidopsis thaliana
2.6.1.14 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 Arabidopsis thaliana
2.6.1.44 dimer crystal structure, enzyme in solution, catalytic enzyme form Arabidopsis thaliana
2.6.1.44 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 Arabidopsis thaliana
2.6.1.45 dimer crystal structure, enzyme in solution, catalytic enzyme form Arabidopsis thaliana
2.6.1.45 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 Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
2.6.1.14 AGT1
-
 Arabidopsis thaliana
2.6.1.14 asparagine aminotransferase
-
 Arabidopsis thaliana
2.6.1.14 asparagine:glyoxylate transaminase
-
 Arabidopsis thaliana
2.6.1.14 More see also EC 2.6.1.45 and 2.6.1.44 Arabidopsis thaliana
2.6.1.44 AGT1
-
 Arabidopsis thaliana
2.6.1.44 alanine:glyoxylate aminotransferase 1
-
 Arabidopsis thaliana
2.6.1.44 More see also EC 2.6.1.45 and 2.6.1.14 Arabidopsis thaliana
2.6.1.45 AGT1
-
 Arabidopsis thaliana
2.6.1.45 More see also EC 2.6.1.44 and 2.6.1.14 Arabidopsis thaliana
2.6.1.45 serine:glyoxylate aminotransferase
-
 Arabidopsis thaliana
2.6.1.45 serine:glyoxylate transaminase
-
 Arabidopsis thaliana
2.6.1.45 SGAT
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.14 pyridoxal 5'-phosphate PLP, is bound at the active site but is not held in place by covalent interactions Arabidopsis thaliana
2.6.1.44 pyridoxal 5'-phosphate PLP, is bound at the active site but is not held in place by covalent interactions Arabidopsis thaliana
2.6.1.45 pyridoxal 5'-phosphate PLP, is bound at the active site but is not held in place by covalent interactions Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
2.6.1.14 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 Arabidopsis thaliana
2.6.1.14 physiological function Arabidopsis thaliana asparagine 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 Arabidopsis thaliana
2.6.1.44 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 Arabidopsis thaliana
2.6.1.44 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 Arabidopsis thaliana
2.6.1.45 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 Arabidopsis thaliana
2.6.1.45 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 Arabidopsis thaliana