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Literature summary extracted from

  • Zhao, A.; Fang, Y.; Chen, X.; Zhao, S.; Dong, W.; Lin, Y.; Gong, W.; Liu, L.
    Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein (2014), Proc. Natl. Acad. Sci. USA, 111, 6630-6635 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.1.70 GluBP regulator the GluTR regulator, GluTR binding protein (GluBP), spatially organizes tetrapyrrole synthesis by distributing enzyme GluTR into different suborganellar locations. GluBP belongs to a heme-binding family involved in heme metabolism. Complex structure of GluTR-GluBP from Arabidopsis thaliana, overview. The dimeric GluBP binds symmetrically to the catalytic domains of the V-shaped GluTR dimer via its C-terminal domain. A substantial conformational change of the GluTR NADPH-binding domain is observed, confirming the postulated rotation of the NADPH-binding domain for hydride transfer from NADPH to the substrate. Arg146, guarding the door for metabolic channeling, adopts alternative conformations, which may represent steps involved in substrate recognition and product release. GluBP stimulates GluTR catalytic efficiency with an approximate 3fold increase of the 5-aminolevulinic acid formation rate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde. GluBP stimulates GluTR activity and regulates GSA release Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.70 purified GluTR in complex with GluBP, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.70 heme feedback inhibition, GluTR activity can be inhibited by heme in a concentration-dependent way regardless of the presence of GluTR binding protein, GluBP 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-glutamyl-tRNAGlu + NADPH + H+ Arabidopsis thaliana
-
 L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.70 L-glutamyl-tRNAGlu + NADPH + H+
-
 Arabidopsis thaliana L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?
1.2.1.70 additional information GluTR employs hydride transfer from NADPH to the thioester-bound glutamate to produce glutamate-1-semialdehyde. The close contact between the nicotinamide ring of NADPH and the nucleophile Cys144 allows the transfer of hydride from NADPH to the thioester-bound glutamate. Tunnel formation in the GluTR-GluBP complex for release of product L-glutamate 1-semialdehyde Arabidopsis thaliana ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.70 GluTR
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.70 NADP+
-
 Arabidopsis thaliana
1.2.1.70 NADPH NADPH-binding model of GluTR by using the homologous structure of a NADP-binding domain Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.2.1.70 physiological function GluTR-catalyzed reaction is the rate-limiting step of tetrapyrrole biosynthesis, and GluTR is the target of multiple posttranslational regulations, such as heme feedback inhibition, for the tetrapyrrole biosynthetic pathway. GluBP stimulates GluTR activity and regulates glutamate 1-semialdehyde release Arabidopsis thaliana