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Literature summary for 1.3.1.33 extracted from

  • Heyes, D.J.; Kruk, J.; Hunter, C.N.
    Spectroscopic and kinetic characterization of the light-dependent enzyme protochlorophyllide oxidoreductase (POR) using monovinyl and divinyl substrates (2006), Biochem. J., 394, 243-248.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information spectroscopic and detailed kinetic characterization of reaction Thermosynechococcus vestitus
0.00083
-
 divinyl protochlorophyllide a pH 7.5 Thermosynechococcus vestitus
0.00136
-
 monovinyl protochlorophyllide a pH 7.5 Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
divinyl protochlorophyllide a + NADPH Thermosynechococcus vestitus
-
 divinyl chlorophyllide a + NADP+
-
 ?
monovinyl protochlorophyllide a + NADPH Thermosynechococcus vestitus
-
 monovinyl chlorophyllide a + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus
-
 srain BP-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
divinyl protochlorophyllide a + NADPH
-
 Thermosynechococcus vestitus divinyl chlorophyllide a + NADP+
-
 ?
monovinyl protochlorophyllide a + NADPH
-
 Thermosynechococcus vestitus monovinyl chlorophyllide a + NADP+
-
 ?