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Literature summary for 1.3.1.33 extracted from

  • Menon, B.R.; Hardman, S.J.; Scrutton, N.S.; Heyes, D.J.
    Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR) (2016), J. Photochem. Photobiol. B, 161, 236-243.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.33

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Thermosynechococcus vestitus

Protein Variants

Protein Variants Comment Organism
G19A the mutant shows wild type value for turnover number Thermosynechococcus vestitus
H236A the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
K42A the mutant shows wild type value for turnover number Thermosynechococcus vestitus
N149V the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
N39V the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
N90A the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
R38V the mutant shows wild type value for turnover number Thermosynechococcus vestitus
S16C the mutant shows wild type value for turnover number Thermosynechococcus vestitus
S189A the mutant shows wild type value for turnover number Thermosynechococcus vestitus
T145A the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
T147F the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
T147S the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
T230A the mutant shows wild type value for turnover number Thermosynechococcus vestitus
T230F the mutant shows reduced value for turnover number compared to the wild type enzyme Thermosynechococcus vestitus
T230S the mutant shows wild type value for turnover number Thermosynechococcus vestitus
Y94F the mutant shows wild type value for turnover number Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus Q8DLC1
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
light-activated enzyme protochlorophyllide oxidoreductase
-
 Thermosynechococcus vestitus
POR
-
 Thermosynechococcus vestitus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.01
-
 protochlorophyllide mutant enzyme N149V, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.01
-
 protochlorophyllide mutant enzyme T145A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.01
-
 protochlorophyllide mutant enzyme T147F, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.01
-
 protochlorophyllide mutant enzyme T230F, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.02
-
 protochlorophyllide mutant enzyme N39V, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.02
-
 protochlorophyllide mutant enzyme T147S, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.07
-
 protochlorophyllide mutant enzyme N90A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.1
-
 protochlorophyllide mutant enzyme H236A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme G19A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme K42A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme R38V, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme S16C, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme S189A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme T230A, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.16
-
 protochlorophyllide mutant enzyme T230S, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.17
-
 protochlorophyllide wild type enzyme, at 25°C, pH not specified in the publication Thermosynechococcus vestitus
0.17
-
 protochlorophyllide mutant enzyme Y94F, at 25°C, pH not specified in the publication Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Thermosynechococcus vestitus