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Ligand 2-aminopropane-1,3-diol Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C3 H9 NO2
2-aminopropane-1,3-diol
KJJPLEZQSCZCKE-UHFFFAOYSA-N
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (4 results)
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serinol + H2O + NAD+ = dihydroxyacetone + NH3 + NADH + H+
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serinol + NAD+ + H2O = dihydroxyacetone + NH3 + NADH + H+
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1,2-dioleoyl-sn-glycerophosphocholine + serinol = choline + 1,2-dioleoyl-sn-glycerophospho-serinol
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2 1,2-dioleoyl-sn-glycerophosphocholine + serinol = 2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-serinol
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Product in Enzyme-catalyzed Reactions (2 results)
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dihydroxyacetone + NH3 + NADH + H+ = serinol + H2O + NAD+
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dihydroxyacetone + NH3 + NADH + H+ = serinol + NAD+ + H2O
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Activator in Enzyme-catalyzed Reactions (2 results)
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activation of aldehyde oxidation
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activation of aldehyde oxidation
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)
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Enzyme Kinetic Parameters
KM Value (2 results)
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References & Links Literature References (4)
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Purification of 2-oxoaldehyde dehydrogenase and its dependence on unusual amines
1975
Dunkerton, J.; James, S.P.
Biochem. J.
149
609-617
Pseudomonas aeruginosa acid phosphatase contains an anionic site with a trimethyl subsite. Kinetic evidence obtained with alkylammonium ions
1988
Garrido, M.N.; Lisa, T.A.; Domenech, C.E.
Mol. Cell. Biochem.
84
41-49
Phospholipase D-catalyzed synthesis of new phospholipids with polar head groups
2008
Dippe, M.; Mrestani-Klaus, C.; Schierhorn, A.; Ulbrich-Hofmann, R.
Chem. Phys. Lipids
152
71-77
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Determining a novel NAD+-dependent amine dehydrogenase with a broad substrate range from Streptomyces Ãirginiae IFO 12827 purification and characterization
2000
Itoh, N.; Yachi, C.; Kudome, T.
J. Mol. Catal. B
10
281-290
Links to other databases for 2-aminopropane-1,3-diol