Literature summary for 1.3.1.33 extracted from

Sameer, H.; Victor, G.; Katalin, S.; Henrik, A.
Elucidation of ligand binding and dimerization of NADPH protochlorophyllide (Pchlide) oxidoreductase from pea (Pisum sativum L.) by structural analysis and simulations (2021), Proteins, 89, 1300-1314 .

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Organism

Organism	UniProt	Comment	Textmining
Pisum sativum	Q01289	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
chlorophyllide a + NADP+	-	Pisum sativum	protochlorophyllide + NADPH + H+	-	?

Subunits

Subunits	Comment	Organism
dimer	dimerization and binding of ligands (both the cofactor NADPH and substrate protochlorophyllide) are computationally investigated the sequence and structural relationships among homologous proteins are identified through database searches. The results indicate that alpha4 and alpha7 helices of monomers form the interface of NADPH:protochlorophyllide oxidoreductase dimers. On the basis of conserved residues, 11 functionally important amino acids that play important roles in binding of the enzyme to NADPH are predicted	Pisum sativum
monomer	the structure of enzyme (POR) protein is predicted in its monomeric and dimeric form	Pisum sativum

Synonyms

Synonyms	Comment	Organism
NADPH:Pchlide oxidoreductase	-	Pisum sativum
NADPH:protochlorophyllide oxidoreductase	-	Pisum sativum
POR	-	Pisum sativum

General Information

General Information	Comment	Organism
physiological function	key enzyme of chlorophyll biosynthesis in angiosperms. Photoenzyme, which catalyzes the light-activated trans-reduction of the C17-C18 double bond of the porphyrin ring of protochlorophyllides. Due to the light requirement, dark-grown angiosperms cannot synthesize chlorophyll	Pisum sativum

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Release 2023.1 (January 2023)