Literature summary for 2.6.1.45 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
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

Localization	Comment	Organism	GeneOntology No.	Textmining
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
L-serine + 3-hydroxypyruvate	Arabidopsis thaliana	-	3-hydroxypyruvate + L-serine	-	?
L-serine + glyoxylate	Arabidopsis thaliana	-	3-hydroxypyruvate + glycine	-	?
L-serine + pyruvate	Arabidopsis thaliana	-	3-hydroxypyruvate + L-alanine	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q56YA5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
L-serine + 3-hydroxypyruvate	-	Arabidopsis thaliana	3-hydroxypyruvate + L-serine	-	?
L-serine + glyoxylate	-	Arabidopsis thaliana	3-hydroxypyruvate + glycine	-	?
L-serine + pyruvate	-	Arabidopsis thaliana	3-hydroxypyruvate + L-alanine	-	?

Subunits

Subunits	Comment	Organism
dimer	crystal structure, enzyme in solution, catalytic enzyme form	Arabidopsis thaliana
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

Synonyms	Comment	Organism
AGT1	-	Arabidopsis thaliana
additional information	see also EC 2.6.1.44 and 2.6.1.14	Arabidopsis thaliana
serine:glyoxylate aminotransferase	-	Arabidopsis thaliana
serine:glyoxylate transaminase	-	Arabidopsis thaliana
SGAT	-	Arabidopsis thaliana

Cofactor

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

General Information

General Information	Comment	Organism
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
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