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Literature summary 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.
    View publication on PubMed

Protein Variants

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.70 Hordeum vulgare
-
-
-

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.70 NADPH
-
 Hordeum vulgare