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Literature summary for 1.3.1.33 extracted from

  • Heyes, D.J.; Menon, B.R.; Sakuma, M.; Scrutton, N.S.
    Conformational events during ternary enzyme-substrate complex formation are rate limiting in the catalytic cycle of the light-driven enzyme protochlorophyllide oxidoreductase (2008), Biochemistry, 47, 10991-10998.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli cells Thermosynechococcus vestitus

Inhibitors

Inhibitors Comment Organism Structure
2',5'-ADP competitive inhibition of NADPH binding Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermosynechococcus vestitus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
POR
-
Thermosynechococcus vestitus
protochlorophyllide oxidoreductase
-
Thermosynechococcus vestitus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
stopped-flow experiments Thermosynechococcus vestitus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
stopped-flow experiments Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Thermosynechococcus vestitus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00302
-
2',5'-ADP calculated competitive inhibition constant Thermosynechococcus vestitus