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Literature summary extracted from

  • Song, Y.; Pu, H.; Jiang, T.; Zhang, L.; Ouyang, M.
    Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thaliana (2016), Acta Crystallogr. Sect. F, 72, 448-456 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.3.8 gene AtGSA1, recombinant expression of His6-tagged enzyme lacking the N-terminal plastid-targeting sequences in Escherichia coli strain BL21(DE3) Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.3.8 purified recombinant detagged enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 200 mM NaCl, with 0.001 ml of reservoir solution containing 0.15 M potassium bromide, and 30% w/v PEG 2000 MME, and equilibration against 0.2 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.25 A resolution Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.4.3.8 chloroplast the enzyme has an N-terminal plastid-targeting sequence Arabidopsis thaliana 9507
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.3.8 L-glutamate 1-semialdehyde Arabidopsis thaliana
-
 5-aminolevulinate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.8 Arabidopsis thaliana P42799
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.3.8 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, removal of the His-tag through TEV protease, followed by gel filtration, and ultrafiltration Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.8 L-glutamate 1-semialdehyde
-
 Arabidopsis thaliana 5-aminolevulinate
-
 ?
5.4.3.8 additional information enzyme GSAM catalyzes the transamination of GSA substrate to form 5-aminolevulinate by an unusual intramolecular exchange of amino and oxo groups via the intermediate 4,5-diaminovalerate (DAVA). The reaction starts with imine formation between pyridoxamine 5'-phosphate and the aldehyde of GSA. During the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation Arabidopsis thaliana ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.3.8 dimer enzyme AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation Arabidopsis thaliana
5.4.3.8 More the overall structure of AtGSA1 consists of three sequentially arranged domains: the N-terminal domain (Val1-Asp63, mature protein) comprises one alpha-helix and a three-stranded antiparallel beta-sheet, the pyridoxamine 5'-phosphate/pyridoxal 5'-phosphate-binding domain (Tyr64-Gly328), which is also the catalytic domain, contains a central seven-stranded beta-sheet with one antiparallel and six parallel beta-strands, and the C-terminal domain (Thr329-Ile434) is composed of a three-stranded antiparallel beta-sheet with four helices covering the outer surface. Asymmetry of AtGSA1 in the gating-loop conformation, overview Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
5.4.3.8 AtGSA1
-
 Arabidopsis thaliana
5.4.3.8 Glutamate-1-semialdehyde aminotransferase
-
 Arabidopsis thaliana
5.4.3.8 glutamate-1-semialdehyde-2,1-aminomutase
-
 Arabidopsis thaliana
5.4.3.8 GSA-AT
-
 Arabidopsis thaliana
5.4.3.8 GSA1
-
 Arabidopsis thaliana
5.4.3.8 GSAM
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.8 additional information during the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation Arabidopsis thaliana
5.4.3.8 pyridoxal 5'-phosphate a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview Arabidopsis thaliana
5.4.3.8 pyridoxamine 5'-phosphate a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
5.4.3.8 additional information structure-function analysis., overview. Enzyme AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation. The mobility of residues Gly163, Ser164 and Gly165 is important for reorientation of the gating loop. The asymmetry of the AtGSA1 structure supports the previously proposed negative cooperativity between monomers of GSAM Arabidopsis thaliana