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Literature summary extracted from

  • Solymosi, K.; Mysliwa-Kurdziel, B.
    The role of membranes and lipid-protein interactions in the Mg-branch of tetrapyrrole biosynthesis (2021), Front. Plant Sci., 12, 663309 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.33 etioplast the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Magnoliopsida 9513
-
1.3.1.33 etioplast the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Arabidopsis thaliana 9513
-
1.3.1.33 etioplast the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Nicotiana tabacum 9513
-
1.3.1.33 etioplast the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Triticum aestivum 9513
-
1.3.1.33 etioplast the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Hordeum vulgare 9513
-
1.3.1.33 etioplast the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Pisum sativum 9513
-
1.3.1.33 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
-
1.3.1.33 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
-
1.3.1.33 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
-
1.3.1.33 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
-
1.3.1.33 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
-
1.3.1.33 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
-
1.3.1.33 thylakoid the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Magnoliopsida 9579
-
1.3.1.33 thylakoid the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Arabidopsis thaliana 9579
-
1.3.1.33 thylakoid the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Nicotiana tabacum 9579
-
1.3.1.33 thylakoid the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Triticum aestivum 9579
-
1.3.1.33 thylakoid the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Hordeum vulgare 9579
-
1.3.1.33 thylakoid the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes Pisum sativum 9579
-

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+ Magnoliopsida
-
chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ Arabidopsis thaliana the enzyme (LPOR) catalyzes a photocatalytic reaction chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ Nicotiana tabacum the enzyme (LPOR) catalyzes a photocatalytic reaction chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ Triticum aestivum the enzyme (LPOR) catalyzes a photocatalytic reaction chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ Hordeum vulgare the enzyme (LPOR) catalyzes a photocatalytic reaction chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ Pisum sativum the enzyme (LPOR) catalyzes a photocatalytic reaction chlorophyllide a + NADP+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.33 Arabidopsis thaliana O48741
-
-
1.3.1.33 Arabidopsis thaliana P21218
-
-
1.3.1.33 Arabidopsis thaliana Q42536
-
-
1.3.1.33 Dinoroseobacter shibae A8LUF3
-
-
1.3.1.33 Hordeum vulgare P13653
-
-
1.3.1.33 Hordeum vulgare Q42850
-
-
1.3.1.33 Magnoliopsida
-
-
-
1.3.1.33 Nicotiana tabacum Q8LSZ2
-
-
1.3.1.33 Nicotiana tabacum Q8LSZ3
-
-
1.3.1.33 Pisum sativum Q01289
-
-
1.3.1.33 Triticum aestivum Q41578
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.33 culture condition:light-deprived cell
-
Pisum sativum
-
1.3.1.33 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
-
1.3.1.33 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
-
1.3.1.33 additional information isoenzyme LPOR-A is present in etiolated tissue Hordeum vulgare
-
1.3.1.33 additional information isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues Magnoliopsida
-
1.3.1.33 additional information isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues Triticum aestivum
-
1.3.1.33 additional information LPOR-B is responsible for the bulk chlorophyll synthesis of adult or green plants Hordeum vulgare
-
1.3.1.33 additional information LPOR-C is expressed typically in green tissues Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.33 protochlorophyllide + NADPH + H+
-
Magnoliopsida chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Magnoliopsida chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Arabidopsis thaliana chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Nicotiana tabacum chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Triticum aestivum chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Hordeum vulgare chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Pisum sativum chlorophyllide a + NADP+
-
?
1.3.1.33 protochlorophyllide + NADPH + H+ the enzyme (LPOR) catalyzes a photocatalytic reaction Dinoroseobacter shibae chlorophyllide a + NADP+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.33 3PCR
-
Pisum sativum
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Magnoliopsida
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Arabidopsis thaliana
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Nicotiana tabacum
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Triticum aestivum
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Hordeum vulgare
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Pisum sativum
1.3.1.33 light-dependent NADPH:protochlorophyllide oxidoreductase
-
Dinoroseobacter shibae
1.3.1.33 LPOR
-
Magnoliopsida
1.3.1.33 LPOR
-
Arabidopsis thaliana
1.3.1.33 LPOR
-
Nicotiana tabacum
1.3.1.33 LPOR
-
Triticum aestivum
1.3.1.33 LPOR
-
Hordeum vulgare
1.3.1.33 LPOR
-
Pisum sativum
1.3.1.33 LPOR
-
Dinoroseobacter shibae
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Magnoliopsida
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Arabidopsis thaliana
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Nicotiana tabacum
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Triticum aestivum
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Hordeum vulgare
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Pisum sativum
1.3.1.33 NADPH:Pchlide oxidoreductase
-
Dinoroseobacter shibae
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Magnoliopsida
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Arabidopsis thaliana
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Nicotiana tabacum
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Triticum aestivum
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Hordeum vulgare
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Pisum sativum
1.3.1.33 NADPH:protochlorophyllide oxidoreductase
-
Dinoroseobacter shibae
1.3.1.33 PAR-A
-
Hordeum vulgare
1.3.1.33 POR-A
-
Arabidopsis thaliana
1.3.1.33 POR-A
-
Triticum aestivum
1.3.1.33 POR-B
-
Arabidopsis thaliana
1.3.1.33 POR-B
-
Hordeum vulgare
1.3.1.33 POR-C
-
Arabidopsis thaliana
1.3.1.33 POR1
-
Nicotiana tabacum
1.3.1.33 POR2
-
Nicotiana tabacum

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Magnoliopsida
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Arabidopsis thaliana
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Nicotiana tabacum
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Triticum aestivum
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Hordeum vulgare
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Pisum sativum
1.3.1.33 additional information light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark Dinoroseobacter shibae

Expression

EC Number Organism Comment Expression
1.3.1.33 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
1.3.1.33 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
1.3.1.33 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
1.3.1.33 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

EC Number General Information Comment Organism
1.3.1.33 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
1.3.1.33 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