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Literature summary for 1.2.1.70 extracted from

  • Fang, Y.; Zhao, S.; Zhang, F.; Zhao, A.; Zhang, W.; Zhang, M.; Liu, L.
    The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein (2016), Sci. Rep., 6, 19756 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
gene HEMA1 Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant GluTR in ternary complex with GBP and FLUTPR, the protein are mixed at molar ratio of 2:3:3, X-ray diffraction structure determination and analysis at 3.2 A resolution, molecular replacement method Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
heme feedback inhibition Arabidopsis thaliana
additional information structure analysis of the FLUTPR-GluTR-GBP ternary complex, overview. Three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP) Arabidopsis thaliana
protein FLU membrane protein FLUORESCENT, protein FLU directly interacts with GluTR's dimerization domain through its tetratricopepetide-repeat (TPR) domain. Enzyme binding structure, overview Arabidopsis thaliana
protein GBP a soluble GluTR-binding protein, enzyme binding structure, overview. the GluTR-GBP complex is stable and has a low apparent dissociation constant. Protein GBP is initially found in chloroplast stroma Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P42804
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More GluTR consists of three domains: an N-terminal catalytic domain, an NADPH-binding domain, and a C-terminal dimerization domain Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
GluTR
-
 Arabidopsis thaliana
HEMA1
-
 Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Arabidopsis thaliana
NADPH
-
 Arabidopsis thaliana

Expression

Organism Comment Expression
Arabidopsis thaliana expression of HEMA1 that encodes the dominant GluTR in the photosynthetic tissues is regulated by light up

General Information

General Information Comment Organism
metabolism plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway1 The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to ALA by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level Arabidopsis thaliana
additional information three mechanisms for plant GluTR activity regulation: (i) the end-product feedback inhibition by heme, (ii) repression by a membrane protein FLUORESCENT (FLU), and (iii) formation of complex with a soluble GluTR-binding protein (GBP) Arabidopsis thaliana
physiological function the GluTR-catalyzed glutamyl-tRNAGlu reduction by NADPH is a key regulatory point of the tetrapyrrole biosynthetic pathway. Plants synthesize delta-aminolevulenic acid (ALA), the precursor for all tetrapyrrole molecules, from glutamate via a three-step pathway. The first step is ligation of glutamate to tRNAGlu catalyzed by glutamyl-tRNA synthetase. Then glutamyl-tRNA reductase (GluTR) reduces the tRNAGlu-bound glutamate to glutamate-1-semialdehyde (GSA) in an NADPH-dependent manner. GSA is subsequently isomerized to 5-aminolevulinic acid by a vitamin B6-dependent enzyme, glutamate-1-semialdehyde aminomutase (GSAM). 5-Aminolevulinic acid synthesis is the key regulatory point for the entire tetrapyrrole biosynthetic pathway, and particularly GluTR is subjected to a tight control at the post-translational level. Regulation of the enzyme within the pathway, detailed overview. Glutamate-1-semialdehyde aminomutase (GSAM) is proposed to form complex with GluTR to enable GSA channeling from GluTR to GSAM in bacteria, but not in plants Arabidopsis thaliana