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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Cofactor
Cofactor on EC 1.2.1.70 - glutamyl-tRNA reductase
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heme
the fusion protein with glutathione S-transferase contains heme, which can be reduced by NADPH and oxidized by air
heme
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enzyme shows Soret peak at 420 nm and a broad absorbance around 540 nm, data suggest that heme is bound preferentially to the dimeric form of GluTR
heme
enzyme preparations with one molecule of heme bound per four GluTR subunits (heme/protein ratio of 1/4) have an increased inactivation rate by H2O2 compared to enzymes with one heme per twelve GluTR subunits (heme/protein ratio of 1/12)
NADPH
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half-maximal rate at 0.005 mM, saturation is not reached even at 10 mM NADH
NADPH
NADPH-binding model of GluTR by using the homologous structure of a NADP-binding domain
the enzyme does not possess a chromophoric prosthetic group
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additional information
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the enzyme does not possess a chromophoric prosthetic group
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