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Literature summary extracted from

  • Zhang, M.; Zhang, F.; Fang, Y.; Chen, X.; Chen, Y.; Zhang, W.; Dai, H.E.; Lin, R.; Liu, L.
    The non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase (2015), J. Biol. Chem., 290, 17559-17565 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.70 gene HEMA1, recombinant co-overexpression of N-terminally His6-tagged FLUTPR and GluTRDD in Escherichia coli strain BL21(DE3) Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.70 uncomplexed TPR domain of FLU (FLUTPR) and complex of the dimeric domain of GluTR bound to FLUTPR, hanging drop vapor diffusion method, from 0.2 M NaCl, 0.1 M Bis-Tris, pH 6.5, and 25% w/v PEG 3350 in 1 week, and from 0.15 M KBr and 30% w/v PEG monomethyl ether 2000, in 3 weeks, X-ray diffraction structure determination and analysis at 1.45 and 2.4 A resolution, respectively, molecular replacement and modeling Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.70 protein FLU the non-canonical tetratricopeptide repeat (TPR) domain of fluorescent (FLU) mediates complex formation with glutamyl-tRNA reductase. Protein FLU negatively regulates glutamyl-tRNA reductase (GluTR) during chlorophyll biosynthesis. A 2:2 FLUTPR-GluTR complex is the functional unit for FLU-mediated GluTR regulation. Enzyme binding complex structure analysis from crystal structures, detailed overview Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.70 L-glutamate 1-semialdehyde + NADP+ + tRNAGlu Arabidopsis thaliana
-
 L-glutamyl-tRNAGlu + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.70 Arabidopsis thaliana P42804
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.70 recombinant N-terminally His6-tagged FLUTPR and GluTRDD in Escherichia coli strain BL21(DE3) Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.70 L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 Arabidopsis thaliana L-glutamyl-tRNAGlu + NADPH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.70 GluTR
-
 Arabidopsis thaliana
1.2.1.70 HEMA1
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.70 NADP+
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.2.1.70 physiological function protein FLU negatively regulates glutamyl-tRNA reductase (GluTR) during chlorophyll biosynthesis. It directly interacts through its TPR domain with glutamyl-tRNA reductase (GluTR), the rate-limiting enzyme in the formation of 5-aminolevulinic acid. The formation of the FLU-GluTR complex prevents glutamyl-tRNA, the GluTR substrate, from binding with this enzyme Arabidopsis thaliana