Ligand (4R)-4-hydroxy-2-oxopentanoate
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Basic Ligand Information
Molecular Structure

C5H8O4
(4R)-4-hydroxy-2-oxopentanoate
HFKQINMYQUXOCH-GSVOUGTGSA-N
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (2 results)
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(4R)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
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(4R)-4-hydroxy-2-oxopentanoate = pyruvate + acetaldehyde
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Product in Enzyme-catalyzed Reactions (1 result)
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pyruvate + acetaldehyde = (4R)-4-hydroxy-2-oxopentanoate
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (6 results)
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0.131
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Y290F mutant protein, pH 8.0, 25°C
0.17
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Y290S mutant protein, pH 8.0, 25°C
0.043
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L87W/Y290F variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.098
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L87N/Y290F variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.131
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Y290F variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.17
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Y290S variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
KM Value (7 results)
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0.012
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Y290S mutant protein, pH 8.0, 25°C
0.013
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Y290F mutant protein, pH 8.0, 25°C
0.012
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Y290S variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.013
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Y290F variant of BphI, app. Km-value, steady-state kinetic parameter, pH 8.0, 25°C
0.013
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Y290F variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.435
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L87W/Y290F variant of BphI, app. Km-value, steady-state kinetic parameter, pH 8.0, 25°C
0.757
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L87N/Y290F variant of BphI, app. Km-value, steady-state kinetic parameter, pH 8.0, 25°C
References & Links
Literature References (2)
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Probing the molecular basis of substrate specificity, stereospecificity, and catalysis in the class II pyruvate aldolase, BphI
2011
Baker, P.; Carere, J.; Seah, S.Y.
Biochemistry
50
3559-3569
Rational design of stereoselectivity in the class II pyruvate aldolase BphI
2012
Baker, P.; Seah, S.Y.K.
J. Am. Chem. Soc.
134
507-513
Links to other databases for (4R)-4-hydroxy-2-oxopentanoate