Literature summary for 1.2.1.70 extracted from

Vothknecht, U.C.; Kannangara, C.G.; von Wettstein, D.
Barley glutamyl tRNAGlu reductase: mutations affecting haem inhibition and enzyme activity (1998), Phytochemistry, 47, 513-519.

Search for more literature for 1.2.1.70

Protein Variants

Protein Variants	Comment	Organism
I318L/R322G/N454D	mutant enzyme with greatly reduced activity	Hordeum vulgare
I464P	mutant enzyme with greatly reduced activity	Hordeum vulgare
L387H/L302S	mutant enzyme with greatly reduced activity	Hordeum vulgare
M122K/K154N/F371L/E400K	mutant enzyme with greatly reduced activity	Hordeum vulgare
additional information	a 30 amino acid N-terminal deletion has no detrimental effect on the catalytic activity of the enzyme	Hordeum vulgare

Inhibitors

Inhibitors	Comment	Organism	Structure
heme	0.002 mM, 63% inhibition of non-truncated enzyme	Hordeum vulgare

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Hordeum vulgare	-	-	-

Substrates and Products (Substrate)

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

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Hordeum vulgare

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Release 2023.1 (January 2023)