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Ligand phylloquinone
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Basic Ligand Information
2-methyl-3-phytyl-1,4-naphthoquinone, 2-methyl-3-[(2E,7R,11R)-3,7,11,15-tetramethylhexadec-2-en-1-yl]naphthalene-1,4-dione, vitamin K, vitamin K1, vitamin K quinone
BRENDA
KEGG
Show all BRENDA pathways known for phylloquinone
close all tables 
open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)
top
EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
phylloquinone + [reduced NADPH-hemoprotein reductase] + O2 = omega-hydroxyphylloquinone + [oxidized NADPH-hemoprotein reductase] + H2O
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phylloquinone + electron donor + O2 = 2,3-epoxyphylloquinone + oxidized electron + H2O
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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In Vivo Product in Enzyme-catalyzed Reactions (6 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O = 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
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vitamin K 2,3-epoxide + dithiothreitol = vitamin K + oxidized dithiothreitol
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S-adenosyl-L-methionine + demethylphylloquinone = S-adenosyl-L-homocysteine + phylloquinone
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Substrate in Enzyme-catalyzed Reactions (16 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
phylloquinone + [reduced NADPH-hemoprotein reductase] + O2 = omega-hydroxyphylloquinone + [oxidized NADPH-hemoprotein reductase] + H2O
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phylloquinone + electron donor + O2 = 2,3-epoxyphylloquinone + oxidized electron + H2O
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phylloquinone + electron donor + O2 = 2,3-epoxyphylloquinone + oxidized electron donor + H2O
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2-methyl-3-phytyl-1,4-naphthoquinone + dithiothreitol = vitamin K hydroquinone + oxidized dithiothreitol
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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vitamin K + 1,4-dithiothreitol = vitamin K hydroquinone + oxidized dithiothreitol + H2O
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2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
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N6-(2-isopentenyl)adenine + vitamin K1 = adenine + 3-methylbut-2-enal + reduced vitamin K1
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2-methyl-3-phytyl-1,4-naphthoquinone + NAD(P)H = 2-methyl-3-phytyl-1,4-naphthohydroquinone + NAD(P)+
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peptidyl-L-glutamate + CO2 + O2 + phylloquinone = peptidyl-4-carboxy L-glutamate + 2,3-epoxyphylloquinone + H2O
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Product in Enzyme-catalyzed Reactions (11 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O = 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
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2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + 1,4-dithiothreitol = vitamin K + oxidized dithiothreitol + H2O
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vitamin K 2,3-epoxide + dithiothreitol = vitamin K + oxidized dithiothreitol
0, 287705, 287706, 287707, 287710, 287711, 287712, 287715, 287716, 287719, 287723, 287713, 287714, 287708, 287717
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vitamin K 2,3-epoxide + reduced dithiothreitol = vitamin K quinone + oxidized dithiothreitol + H2O
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S-adenosyl-L-methionine + demethylphylloquinone = S-adenosyl-L-homocysteine + phylloquinone
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Enzyme Cofactor/Cosubstrate (313 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower
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photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
photosystem I (PS I) mediates electron-transfer from plastocyanin to ferredoxin via a photochemically active chlorophyll dimer (P700), a monomeric chlorophyll electron acceptor (A0), a phylloquinone (A1), and three [4Fe-4S] clusters (FX/A/B)
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
the PSI complex of cyanobacteria and chloroplasts contains two phylloquinone molecules, which function in the electron transfer as the redox center A1
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672089, 696271, 699860, 715657, 716953, 726845, 695615, 696951, 699400, 701112, 438307, 438309, 696184, 697924, 698697, 698705, 701022, 701296, 695976, 695978, 697786, 700930, 716060
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carboxylase and soybean seed lipoxygenase share 19.3% identity over a span of 198 amino acids, from residues 468 to 666 of carboxylase. This is interesting because the carboxylase acts as an oxygenase on the cofactor vitamin K-hydroquinone, and the similarity occurs in that region of the carboxylase likely to have enzymatic function
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conversion of glutamic acid to gamma-carboxyglutamic acid is coupled with the oxygenation of KH2 to vitamin K 2,3-epoxide and has been referred to as vitamin K epoxidase activity
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the carboxylase uses the energy of vitamin K hydroquinone oxygenation to convert glutamyl residues to gamma-carboxylated glutamyl residues in vitamin Kâdependent proteins. During carboxylation, the vitamin K hydroquinone cofactor is oxidized to a vitamin K epoxide product
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the enzyme requires vitamin K as a cofactor for its post-translational modification of glutamic acid residues to gamma-carboxyglutamic acid residues
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Activator in Enzyme-catalyzed Reactions (6 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
Inhibitor in Enzyme-catalyzed Reactions (6 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
carboxylation of FLEEL by bovine liver carboxylase is inhibited by high concentrations of vitamin KH2. vitamin K (up to 400 mM) and vitamin K epoxide (up to 1 mM) are not inhibitory. R234A/H235A mutant, R406A/H408A mutant, and R513A/K515A mutant are more susceptible to inhibition by vitamin KH2 than wild type enzyme. R234A/H235A mutant and R406A/H408A mutant exhibit maximal activity at 111 mM vitamin KH2 and R513A/K515A mutant at 56 mM vitamin KH2
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3D Structure of Enzyme-Ligand-Complex (PDB) (445 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (1 result)
EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
KM Value (7 results)
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0072
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recombinant wild-type enzyme in recombinant Pichia pastoris membranes, pH 7.4, 37°C
IC50 Value (2 results)
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
References & Links
Literature References (111)
Links to other databases for phylloquinone
ChEBI
PubChem
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Release 2023.1 (January 2023)
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