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Literature summary for 1.3.1.33 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
Search for more literature for 1.3.1.33

Protein Variants

Protein Variants Comment Organism
F233L mutant enzyme shows around 40% of wild-type activity Thermosynechococcus vestitus
F233Y mutant enzyme shows around 40% of wild-type activity Thermosynechococcus vestitus
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
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
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
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
POR
-
 Thermosynechococcus vestitus

Turnover Number [1/s]

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

General Information

General Information Comment Organism
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