Literature summary extracted from

Archipowa, N.; Kutta, R.J.; Heyes, D.J.; Scrutton, N.S.
Stepwise hydridet transfer in a biological system insights into the reaction mechanism of the light-dependent protochlorophyllide oxidoreductase (2018), Angew. Chem. Int. Ed. Engl., 57, 2682-2686 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.3.1.33	subcloned into the expression vector pRSETA and recombinantly expressed in Escherichia coli SoluBL21	Thermosynechococcus vestitus

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.3.1.33	C226S	the formed protochlorophyllide species in C226S must differ compared to those formed in wild-type enzyme, for example, by attachment of the hydride at C18 rather than C17	Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.3.1.33	protochlorophyllide + NADPH + H+	Thermosynechococcus vestitus	-	chlorophyllide a + NADP+	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.3.1.33	Thermosynechococcus vestitus	Q8DLC1	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.3.1.33	protochlorophyllide + NADPH + H+	-	Thermosynechococcus vestitus	chlorophyllide a + NADP+	-	?
1.3.1.33	protochlorophyllide + NADPH + H+	stepwise hydride transfer. The enzyme catalyzes the stereospecific trans addition of a hydride anion and a proton across the C17-C18 double bond of protochlorophyllide	Thermosynechococcus vestitus	chlorophyllide a + NADP+	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.3.1.33	Light-dependent protochlorophyllide oxidoreductase	-	Thermosynechococcus vestitus
1.3.1.33	POR	-	Thermosynechococcus vestitus

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.3.1.33	NADPH	-	Thermosynechococcus vestitus

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Release 2023.1 (January 2023)