BRENDA - Enzyme Database

Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein

Zhao, A.; Fang, Y.; Chen, X.; Zhao, S.; Dong, W.; Lin, Y.; Gong, W.; Liu, L.; Proc. Natl. Acad. Sci. USA 111, 6630-6635 (2014)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Arabidopsis thaliana
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.70
Arabidopsis thaliana
P42804
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
743681
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
743681
Arabidopsis thaliana
?
-
-
-
-
Cofactor
EC Number
Cofactor
Commentary
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
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
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 (protein specific)
EC Number
Inhibitors
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Arabidopsis thaliana
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
743681
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
743681
Arabidopsis thaliana
?
-
-
-
-
General Information
EC Number
General Information
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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