Protochlorophyllide reductase

protochlorophyllide reductase
Identifiers
EC number 1.3.1.33
CAS number 68518-04-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a protochlorophyllide reductase (EC 1.3.1.33) is an enzyme that catalyzes the chemical reaction

protochlorophyllide + NADPH + H+ chlorophyllide a + NADP+

Thus, the three substrates of this enzyme are protochlorophyllide, NADPH, and H+, whereas its 2 products are chlorophyllide a and NADP+ .

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is chlorophyllide-a:NADP+ 7,8-oxidoreductase. Other names in common use include NADPH2-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide reductase, protochlorophyllide oxidoreductase, and protochlorophyllide photooxidoreductase. This enzyme participates in porphyrin and chlorophyll metabolism.

There are two structurally unrelated proteins with this activity, referred to as light-dependent and the dark-operative. The light-dependent reductase needs light to function, while the dark-operative version is a completely different protein, consisting of three subunits that exhibit significant sequence similarity to the three subunits of nitrogenase.[1] This enzyme might be evolutionary older but (being similar to nitrogenase) is highly sensitive to free oxygen and does not work if its concentration exceeds about 3%.[2] Hence the alternative, light dependent version needed to evolve.

References

  1. Yuichi FujitaDagger and Carl E. Bauer (2000). Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits. J. Biol. Chem., Vol. 275, Issue 31, 23583-23588.
  2. S.Yamazaki, J.Nomata, Y.Fujita (2006) Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana. Plant Physiology, 2006, 142, 911-922


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