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 |
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 |
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 | - |
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 | - |
? |
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 | - |
- |
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 | - |
? |
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 |
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 |
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 |
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 |