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Literature summary extracted from

  • Zhang, S.; Godwin, A.R.F.; Taylor, A.; Hardman, S.J.O.; Jowitt, T.A.; Johannissen, L.O.; Hay, S.; Baldock, C.; Heyes, D.J.; Scrutton, N.S.
    Dual role of the active site lid regions of protochlorophyllide oxidoreductase in photocatalysis and plant development (2021), FEBS J., 288, 175-189 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.33 F233L mutant enzyme shows around 40% of wild-type activity Thermosynechococcus vestitus
1.3.1.33 F233Y mutant enzyme shows around 40% of wild-type activity Thermosynechococcus vestitus
1.3.1.33 F237Y as in the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is red-shifted by about 12 nm compared to free protochlorophyllide Thermosynechococcus vestitus
1.3.1.33 F240Y distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide Thermosynechococcus vestitus
1.3.1.33 F244Y distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide Thermosynechococcus vestitus
1.3.1.33 F247Y distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide Thermosynechococcus vestitus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.33 0.0008
-
 NADPH pH 7.5, 40°C, mutant enzyme P158F Thermosynechococcus vestitus
1.3.1.33 0.0009
-
 NADPH pH 7.5, 40°C, wild-type enzyme Thermosynechococcus vestitus
1.3.1.33 0.001
-
 NADPH pH 7.5, 40°C, mutant enzyme F233Y Thermosynechococcus vestitus
1.3.1.33 0.0022
-
 NADPH pH 7.5, 40°C, mutant enzyme K156N/I157V Thermosynechococcus vestitus
1.3.1.33 0.0025
-
 NADPH pH 7.5, 40°C, mutant enzyme F237Y Thermosynechococcus vestitus
1.3.1.33 0.0029
-
 NADPH pH 7.5, 40°C, mutant enzyme F233L Thermosynechococcus vestitus
1.3.1.33 0.0029
-
 NADPH pH 7.5, 40°C, mutant enzyme I157V Thermosynechococcus vestitus
1.3.1.33 0.0029
-
 NADPH pH 7.5, 40°C, mutant enzyme K156N Thermosynechococcus vestitus
1.3.1.33 0.0033
-
 NADPH pH 7.5, 40°C, mutant enzyme P158A Thermosynechococcus vestitus
1.3.1.33 0.0069
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme F237Y Thermosynechococcus vestitus
1.3.1.33 0.0075
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme F233L Thermosynechococcus vestitus
1.3.1.33 0.0078
-
 protochlorophyllide pH 7.5, 40°C, wild-type enzyme Thermosynechococcus vestitus
1.3.1.33 0.0081
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme F233Y Thermosynechococcus vestitus
1.3.1.33 0.0107
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme I157V Thermosynechococcus vestitus
1.3.1.33 0.0135
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme P158A Thermosynechococcus vestitus
1.3.1.33 0.0151
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme K156N Thermosynechococcus vestitus
1.3.1.33 0.0166
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme K156N/I157V Thermosynechococcus vestitus
1.3.1.33 0.0181
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme P158F Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.33 protochlorophyllide + NADPH + H+ Thermosynechococcus vestitus light-dependent reaction of chlorophyll biosynthesis chlorophyllide a + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.33 Thermosynechococcus vestitus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.33 protochlorophyllide + NADPH + H+ light-dependent reaction of chlorophyll biosynthesis Thermosynechococcus vestitus chlorophyllide a + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.33 oligomer protochlorophyllide binding triggers formation of large oligomers of the enzyme (POR). Oligomer formation is most likely driven by the interaction of amino acid residues in the highly conserved lid regions. The lid residues position protochlorophyllide optimally to enable photocatalysis. Following protochlorophyllide binding, they also enable POR oligomerisation - a process that is reversed through subsequent photocatalysis in the early stages of chloroplast development Thermosynechococcus vestitus

Synonyms

EC Number Synonyms Comment Organism
1.3.1.33 POR
-
 Thermosynechococcus vestitus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.33 0.007
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme F233L Thermosynechococcus vestitus
1.3.1.33 0.013
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme F233Y Thermosynechococcus vestitus
1.3.1.33 0.013
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme P158F Thermosynechococcus vestitus
1.3.1.33 0.022
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme K156N/I157V Thermosynechococcus vestitus
1.3.1.33 0.027
-
 protochlorophyllide pH 7.5, 40°C, wild-type enzyme Thermosynechococcus vestitus
1.3.1.33 0.03
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme F237Y Thermosynechococcus vestitus
1.3.1.33 0.035
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme K156N Thermosynechococcus vestitus
1.3.1.33 0.037
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme I157V Thermosynechococcus vestitus
1.3.1.33 0.037
-
 protochlorophyllide pH 7.5, 40°C, mutant enzyme P158A Thermosynechococcus vestitus

General Information

EC Number General Information Comment Organism
1.3.1.33 physiological function light-dependent reaction of chlorophyll biosynthesis. The enzyme (POR) is also important in plant development as it is the main constituent of prolamellar bodies in etioplast membranes Thermosynechococcus vestitus