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Ligand 2-2H-4-allohydroxy-D-Pro Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C5 H9 NO3
2-2H-4-allohydroxy-D-Pro
PMMYEEVYMWASQN-QWWZWVQMSA-N
4-allohydroxy-D-Pro, allo-4-hydroxy-D-proline, Allohydroxy-D-Pro, cis-4-Hydroxy-D-Pro, cis-4-hydroxy-D-proline
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)
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cis-4-hydroxy-D-proline + acceptor = (4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate + reduced acceptor
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In Vivo Product in Enzyme-catalyzed Reactions (1 result)
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trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
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Substrate in Enzyme-catalyzed Reactions (4 results)
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cis-4-hydroxy-D-proline + acceptor = (4R)-DELTA1-pyrroline-4-hydroxy-2-carboxylate + reduced acceptor
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allo-4-hydroxy-D-proline + oxidized 2,6-dichloroindophenol + H2O = ? + reduced 2,6-dichloroindophenol
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Allohydroxy-D-Pro = Allohydroxy-L-Pro
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cis-4-hydroxy-D-proline = trans-4-hydroxy-L-proline
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Product in Enzyme-catalyzed Reactions (2 results)
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trans-4-hydroxy-L-Pro = cis-4-hydroxy-D-Pro
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trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline
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3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (4 results)
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0.014
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pH 8.0, 50°C, mutant enzyme F62S
0.11
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pH 8.0, 50°C, mutant enzyme L221H
0.69
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pH 8.0, 50°C, mutant enzyme W241F
3.83
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pH 8.0, 50°C, wild-type enzyme
KM Value (9 results)
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0.0628
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pH 8.0, 30°C, AbLhpBEF protein
3.14
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pH 8.0, 50°C, mutant enzyme F62S
4.18
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pH 8.0, 50°C, mutant enzyme L221H
6.65
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pH 8.0, 50°C, wild-type enzyme
6.7
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pH 8.0, 50°C, mutant enzyme W241F
8
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pH not specified in the publication, 30°C, recombinant enzyme
References & Links Literature References (6)
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Purification and properties of inducible hydroxyproline 2-epimerase from Pseudomonas
1964
Adams, E.; Norton, I.L.
J. Biol. Chem.
239
1525-1535
Kinetic and structural studies of hydroxyproline 2-epimerase
1970
Finlay, T.H.; Adams, E.
J. Biol. Chem.
245
5248-5260
Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase
2002
Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T.
J. Biol. Chem.
277
12861-12867
Control of hydroxyproline catabolism in Sinorhizobium meliloti
2012
White, C.E.; Gavina, J.M.; Morton, R.; Britz-McKibbin, P.; Finan, T.M.
Mol. Microbiol.
85
1133-1147
Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution
2015
Watanabe, S.; Tanimoto, Y.; Nishiwaki, H.; Watanabe, Y.
PLoS One
10
e0120349
An enzymatic method to estimate the content of L-hydroxyproline
2015
Watanabe, S.; Hiraoka, Y.; Endo, S.; Tanimoto, Y.; Tozawa, Y.; Watanabe, Y.
J. Biotechnol.
199
9-16
Links to other databases for 2-2H-4-allohydroxy-D-Pro