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Literature summary for 1.2.1.70 extracted from

  • Chen, M.W.; Jahn, D.; O'Neill, G.P.; Soll, D.
    Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis (1990), J. Biol. Chem., 265, 4058-4063.
    View publication on PubMed
Search for more literature for 1.2.1.70

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
 glycerol gradient sedimentation, gel filtration Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamyl-tRNAGlu + NADPH + H+ Chlamydomonas reinhardtii the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Chlamydomonas reinhardtii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamyl-tRNAGlu + NADPH + H+
-
 Chlamydomonas reinhardtii L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?
L-glutamyl-tRNAGlu + NADPH + H+ the enzyme is involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis Chlamydomonas reinhardtii L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 130000, SDS-PAGE Chlamydomonas reinhardtii

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Chlamydomonas reinhardtii