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Literature summary for 1.2.1.70 extracted from

  • Moser, J.; Lorenz, S.; Hubschwerlen, C.; Rompf, A.; Jahn, D.
    Methanopyrus kandleri glutamyl-tRNA reductase (1999), J. Biol. Chem., 274, 30679-30685.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Methanopyrus kandleri

Protein Variants

Protein Variants Comment Organism
C393S 95% of the GluTR reductase activity compared to wild-type enzyme, 100% of the GluTR esterase activity compared to wild-type enzyme Methanopyrus kandleri
C42S no GluTR reductase and GluTR esterase activity Methanopyrus kandleri
C48S 90% of the GluTR reductase activity compared to wild-type enzyme, 95% of the GluTR esterase activity compared to wild-type enzyme Methanopyrus kandleri
C6S 130% of the GluTR reductase activity compared to wild-type enzyme, 120% of the GluTR esterase activity compared to wild-type enzyme Methanopyrus kandleri
C90S 85% of the GluTR reductase activity compared to wild-type enzyme, 105% of the GluTR esterase activity compared to wild-type enzyme Methanopyrus kandleri
H84A no GluTR reductase activity, 5% of the GluTR esterase activity compared to wild-type enzyme Methanopyrus kandleri
H84N 30% of the GluTR reductase activity compared to wild-type enzyme, 15% of the GluTR esterase activity compared to wild-type enzyme Methanopyrus kandleri

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoic acid) 1.0 mM, 90% inhibition Methanopyrus kandleri
glutamate-1-semialdehyde 1.0 mM, 50% inhibition Methanopyrus kandleri
glutamycin 2.5 mM, 75% inhibition Methanopyrus kandleri
heme 0.007 mM, 70% inhibition Methanopyrus kandleri
iodoacetamide 0.01 mM, 30% inhibition, 0.1 mM, complete inhibition Methanopyrus kandleri
N-tosyl-L-phenylalaninechloromethyl ketone 0.1 mM, 90% inhibition, 1.0 mM, complete inhibition Methanopyrus kandleri
PbCl2 0.1 mM, 60% inhibition, 1.0 mM, complete inhibition Methanopyrus kandleri
PtCl4 0.1 mM, 55% inhibition, 1.0 mM, 90% inhibition Methanopyrus kandleri
ZnCl2 0.2 mM, 45% inhibition, 5.0 mM, 90% inhibition Methanopyrus kandleri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45436
-
x * 45436, electrospray ionization mass spectrometry Methanopyrus kandleri
190000
-
gel filtration Methanopyrus kandleri

Organism

Organism UniProt Comment Textmining
Methanopyrus kandleri Q9UXR8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanopyrus kandleri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamyl-tRNAGlu + NADPH + H+ in absence of NADPH, an esterase activity of GluTR hydrolyzes the highly reactive thioester of tRNAGlu to release glutamate Methanopyrus kandleri L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
?

Subunits

Subunits Comment Organism
? x * 45436, electrospray ionization mass spectrometry Methanopyrus kandleri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
-
Methanopyrus kandleri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
-
Methanopyrus kandleri

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme does not possess a chromophoric prosthetic group Methanopyrus kandleri
NADPH
-
Methanopyrus kandleri

pI Value

Organism Comment pI Value Maximum pI Value
Methanopyrus kandleri isoelectric focusing
-
6