Literature summary for 1.2.1.70 extracted from

Schubert, W.D.; Moser, J.; Schauer, S.; Heinz, D.W.; Jahn, D.
Structure and function of glutamyl-tRNA reductase, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes (2002), Photosynth. Res., 74, 205-215 (c).

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallized in presence of glutamycin, the structure is solved by the multiple isomorphous replacement method using three heavy atom derivatives. The structure is subsequently refined at a resolution of 1.95 A	Methanopyrus kandleri

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-glutamyl-tRNAGlu + NADPH + H+	Methanopyrus kandleri	the enzyme catalyzes the initial step of tetrapyrrole biosynthesis	L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanopyrus kandleri	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamyl-tRNAGlu + NADPH + H+	-	Methanopyrus kandleri	L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	-	?
L-glutamyl-tRNAGlu + NADPH + H+	the enzyme catalyzes the initial step of tetrapyrrole biosynthesis	Methanopyrus kandleri	L-glutamate 1-semialdehyde + NADP+ + tRNAGlu	-	?

Synonyms

Synonyms	Comment	Organism
GluTR	-	Methanopyrus kandleri

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Methanopyrus kandleri

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Release 2023.1 (January 2023)