1.2.1.70: glutamyl-tRNA reductase
This is an abbreviated version!
For detailed information about glutamyl-tRNA reductase, go to the full flat file.
Word Map on EC 1.2.1.70
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1.2.1.70
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tetrapyrrole
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chlorophyl
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ala
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5-aminolevulinic
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heme
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glutamate-1-semialdehyde
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protochlorophyllide
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delta-aminolevulinic
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1-semialdehyde
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de-etiolation
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chelatase
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mg-protoporphyrin
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glu-trna
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trna-dependent
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kandleri
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pchlide
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gun4
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glu-trnaglu
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trna-bound
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2,1-aminomutase
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biotechnology
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synthesis
- 1.2.1.70
- tetrapyrrole
-
chlorophyl
- ala
-
5-aminolevulinic
- heme
- glutamate-1-semialdehyde
- protochlorophyllide
-
delta-aminolevulinic
- 1-semialdehyde
-
de-etiolation
- chelatase
- mg-protoporphyrin
- glu-trna
-
trna-dependent
- kandleri
-
pchlide
- gun4
- glu-trnaglu
-
trna-bound
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2,1-aminomutase
- biotechnology
- synthesis
Reaction
Synonyms
AtHEMA1, EC 2.7.2.13, GluRS, glutamate tRNA reductase, glutamate-specific tRNA reductase, glutamyl transfer RNA reductase, glutamyl-tRNA reductase, GluTR, GluTR1, GTR, GtrR, hemA, HEMA1, HEMA2, reductase, glutamyl-transfer ribonucleate, ZjGluTR
ECTree
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Inhibitors
Inhibitors on EC 1.2.1.70 - glutamyl-tRNA reductase
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2,4-diphenyl-6-styryl-1-p-tolyl-pyridinium boron tetrafluoride
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IC50: 0.01 mM
4-[4-(3,4-dihydroxyphenyl)-2,3-dimethylbutyl]benzene-1,2-diol
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IC50: 0.055 mM
fluorescent in blue light
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FLU, the protein mediates inactivation of the enzyme at the membrane
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H2O2
inactivates the enzyme. H2O2 decreases the stimulation of GluTR by glutamate semialdehyde 1-2 aminomutase, GSAM
N-tosyl-L-phenylalaninechloromethyl ketone
0.1 mM, 90% inhibition, 1.0 mM, complete inhibition
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
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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)
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when intracellular heme is in excess, the cells respond by a dramatic decrease of the level of GluTR
heme
feedback inhibition, GluTR activity can be inhibited by heme in a concentration-dependent way regardless of the presence of GluTR binding protein, GluBP
iodoacetamide
0.01 mM, 30% inhibition, 0.1 mM, complete inhibition
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
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protein FLU
membrane protein FLUORESCENT, protein FLU directly interacts with GluTR's dimerization domain through its tetratricopepetide-repeat (TPR) domain. Enzyme binding structure, overview
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