Literature summary for 1.3.1.33 extracted from

Sytina, O.A.; Heyes, D.J.; Hunter, C.N.; Groot, M.L.
Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR) (2009), Biochem. Soc. Trans., 37, 387-391.

Search for more literature for 1.3.1.33

Protein Variants

Protein Variants	Comment	Organism
Y189F	mutant, the putative proton donor, Tyr 189, is replaced by a phenylalanine residue	Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
protochlorophyllide + NADPH + H+	Synechocystis sp.	activation by light	chlorophyllide + NADP+	-	?

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
protochlorophyllide + NADPH + H+	activation by light	Synechocystis sp.	chlorophyllide + NADP+	-	?

Synonyms

Synonyms	Comment	Organism
POR	-	Synechocystis sp.
protochlorophyllide oxidoreductase	-	Synechocystis sp.

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Synechocystis sp.

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)