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Literature summary for 1.3.1.33 extracted from

  • Menon, B.R.; Waltho, J.P.; Scrutton, N.S.; Heyes, D.J.
    Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductase (2009), J. Biol. Chem., 284, 18160-18166.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.33

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
K197A mutant, constructed for analysing the role of the conserved active site lysine Thermosynechococcus vestitus
K197Q mutant, constructed for analysing the role of the conserved active site lysine Thermosynechococcus vestitus
K197R mutant, constructed for analysing the role of the conserved active site lysine Thermosynechococcus vestitus
Y193A mutant, constructed for analysing the role of the conserved active site tyrosine Thermosynechococcus vestitus
Y193F mutant, constructed for analysing the role of the conserved active site tyrosine Thermosynechococcus vestitus
Y193S mutant, constructed for analysing the role of the conserved active site tyrosine Thermosynechococcus vestitus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 protochlorophyllide mutant K197A, relative activity 2.7% Thermosynechococcus vestitus
additional information
-
 protochlorophyllide mutant K197Q, relative activity 2.0% Thermosynechococcus vestitus
additional information
-
 protochlorophyllide mutant K197R, relative activity 2.3% Thermosynechococcus vestitus
additional information
-
 protochlorophyllide mutant Y193A, relative activity 5.5% Thermosynechococcus vestitus
additional information
-
 protochlorophyllide mutant Y193F, relative activity 19.5% Thermosynechococcus vestitus
additional information
-
 protochlorophyllide mutant Y193S, relative activity 2.4% Thermosynechococcus vestitus
additional information
-
 protochlorophyllide wild type enzyme, relative activity 100% 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
-
 activity assay Thermosynechococcus vestitus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.003
-
 protochlorophyllide mutant K197Q Thermosynechococcus vestitus
0.004
-
 protochlorophyllide mutant K197A Thermosynechococcus vestitus
0.004
-
 protochlorophyllide mutant K197R Thermosynechococcus vestitus
0.004
-
 protochlorophyllide mutant Y193S Thermosynechococcus vestitus
0.009
-
 protochlorophyllide mutant Y193A Thermosynechococcus vestitus
0.032
-
 protochlorophyllide mutant Y193F Thermosynechococcus vestitus
0.164
-
 protochlorophyllide wild type enzyme Thermosynechococcus vestitus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 activity assay Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Thermosynechococcus vestitus