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Literature summary for 1.3.1.33 extracted from
- The role of membranes and lipid-protein interactions in the Mg-branch of tetrapyrrole biosynthesis (2021), Front. Plant Sci., 12, 663309 .
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| etioplast | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Magnoliopsida | 9513 | - |
| etioplast | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Arabidopsis thaliana | 9513 | - |
| etioplast | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Nicotiana tabacum | 9513 | - |
| etioplast | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Triticum aestivum | 9513 | - |
| etioplast | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Hordeum vulgare | 9513 | - |
| etioplast | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Pisum sativum | 9513 | - |
| membrane | LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane | Magnoliopsida | 16020 | - |
| membrane | LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane | Arabidopsis thaliana | 16020 | - |
| membrane | LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane | Nicotiana tabacum | 16020 | - |
| membrane | LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane | Triticum aestivum | 16020 | - |
| membrane | LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane | Hordeum vulgare | 16020 | - |
| membrane | LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane | Pisum sativum | 16020 | - |
| thylakoid | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Magnoliopsida | 9579 | - |
| thylakoid | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Arabidopsis thaliana | 9579 | - |
| thylakoid | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Nicotiana tabacum | 9579 | - |
| thylakoid | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Triticum aestivum | 9579 | - |
| thylakoid | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Hordeum vulgare | 9579 | - |
| thylakoid | the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes | Pisum sativum | 9579 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protochlorophyllide + NADPH + H+ | Magnoliopsida | - |
chlorophyllide a + NADP+ | - |
? |  |
| protochlorophyllide + NADPH + H+ | Arabidopsis thaliana | the enzyme (LPOR) catalyzes a photocatalytic reaction | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | Nicotiana tabacum | the enzyme (LPOR) catalyzes a photocatalytic reaction | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | Triticum aestivum | the enzyme (LPOR) catalyzes a photocatalytic reaction | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | Hordeum vulgare | the enzyme (LPOR) catalyzes a photocatalytic reaction | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | Pisum sativum | the enzyme (LPOR) catalyzes a photocatalytic reaction | chlorophyllide a + NADP+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | O48741 | - |
- |
| Arabidopsis thaliana | P21218 | - |
- |
| Arabidopsis thaliana | Q42536 | - |
- |
| Dinoroseobacter shibae | A8LUF3 | - |
- |
| Hordeum vulgare | P13653 | - |
- |
| Hordeum vulgare | Q42850 | - |
- |
| Magnoliopsida | - |
- |
- |
| Nicotiana tabacum | Q8LSZ2 | - |
- |
| Nicotiana tabacum | Q8LSZ3 | - |
- |
| Pisum sativum | Q01289 | - |
- |
| Triticum aestivum | Q41578 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture condition:light-deprived cell | - |
Pisum sativum | - |
| etiolated plant tissue | LPOR-A is present in etiolated tissue. LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants | Arabidopsis thaliana | - |
| etiolated plant tissue | LPOR-B is present in etiolated tissue. LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants | Arabidopsis thaliana | - |
| additional information | isoenzyme LPOR-A is present in etiolated tissue | Hordeum vulgare | - |
| additional information | isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues | Magnoliopsida | - |
| additional information | isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues | Triticum aestivum | - |
| additional information | LPOR-B is responsible for the bulk chlorophyll synthesis of adult or green plants | Hordeum vulgare | - |
| additional information | LPOR-C is expressed typically in green tissues | Arabidopsis thaliana | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protochlorophyllide + NADPH + H+ | - |
Magnoliopsida | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Magnoliopsida | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Arabidopsis thaliana | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Nicotiana tabacum | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Triticum aestivum | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Hordeum vulgare | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Pisum sativum | chlorophyllide a + NADP+ | - |
? | |
| protochlorophyllide + NADPH + H+ | the enzyme (LPOR) catalyzes a photocatalytic reaction | Dinoroseobacter shibae | chlorophyllide a + NADP+ | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 3PCR | - |
Pisum sativum |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Magnoliopsida |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Arabidopsis thaliana |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Nicotiana tabacum |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Triticum aestivum |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Hordeum vulgare |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Pisum sativum |
| light-dependent NADPH:protochlorophyllide oxidoreductase | - |
Dinoroseobacter shibae |
| LPOR | - |
Magnoliopsida |
| LPOR | - |
Arabidopsis thaliana |
| LPOR | - |
Nicotiana tabacum |
| LPOR | - |
Triticum aestivum |
| LPOR | - |
Hordeum vulgare |
| LPOR | - |
Pisum sativum |
| LPOR | - |
Dinoroseobacter shibae |
| NADPH:Pchlide oxidoreductase | - |
Magnoliopsida |
| NADPH:Pchlide oxidoreductase | - |
Arabidopsis thaliana |
| NADPH:Pchlide oxidoreductase | - |
Nicotiana tabacum |
| NADPH:Pchlide oxidoreductase | - |
Triticum aestivum |
| NADPH:Pchlide oxidoreductase | - |
Hordeum vulgare |
| NADPH:Pchlide oxidoreductase | - |
Pisum sativum |
| NADPH:Pchlide oxidoreductase | - |
Dinoroseobacter shibae |
| NADPH:protochlorophyllide oxidoreductase | - |
Magnoliopsida |
| NADPH:protochlorophyllide oxidoreductase | - |
Arabidopsis thaliana |
| NADPH:protochlorophyllide oxidoreductase | - |
Nicotiana tabacum |
| NADPH:protochlorophyllide oxidoreductase | - |
Triticum aestivum |
| NADPH:protochlorophyllide oxidoreductase | - |
Hordeum vulgare |
| NADPH:protochlorophyllide oxidoreductase | - |
Pisum sativum |
| NADPH:protochlorophyllide oxidoreductase | - |
Dinoroseobacter shibae |
| PAR-A | - |
Hordeum vulgare |
| POR-A | - |
Arabidopsis thaliana |
| POR-A | - |
Triticum aestivum |
| POR-B | - |
Arabidopsis thaliana |
| POR-B | - |
Hordeum vulgare |
| POR-C | - |
Arabidopsis thaliana |
| POR1 | - |
Nicotiana tabacum |
| POR2 | - |
Nicotiana tabacum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Magnoliopsida | |
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Arabidopsis thaliana | |
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Nicotiana tabacum | |
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Triticum aestivum | |
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Hordeum vulgare | |
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Pisum sativum | |
| additional information | light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark | Dinoroseobacter shibae |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Magnoliopsida | isoform LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while isoform LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants | up |
| Arabidopsis thaliana | LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants | up |
| Triticum aestivum | LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants | up |
| Hordeum vulgare | LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | oxygen-sensitive dark-operative NADPH:Pchlide oxidoreductase enzyme (DPOR) and light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) show very low sequence homology. In most organisms they occur simultaneously. However, angiosperms lack LPOR and became unable to synthesize chlorophyllides and chlorophylls (Chls) in the absence of light | Magnoliopsida |
| evolution | oxygen-sensitive dark-operative NADPH:Pchlide oxidoreductase enzyme (DPOR) and light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) show very low sequence homology. In most organisms they occur simultaneously. However, angiosperms lack LPOR and became unable to synthesize chlorophyllides and chlorophylls (Chls) in the absence of light | Hordeum vulgare |
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Release 2023.1 (January 2023)
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