Neha Patil (Editor)

Protochlorophyllide reductase

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EC number
  
1.3.1.33

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
68518-04-7

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

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. 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%. Hence the alternative, light dependent version needed to evolve.

References

Protochlorophyllide reductase Wikipedia