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Information on EC 1.1.1.313 - sulfoacetaldehyde reductase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Chromohalobacter salexigens
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sulfoacetaldehyde reductase
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isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+
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Taurine and hypotaurine metabolism
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sulfoacetaldehyde degradation III
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isethionate:NADP+ oxidoreductase
Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells.
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isethionate formation, reductase D
NADPH-dependent sulfoacetaldehyde reductase
isethionate formation, reductase D
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isethionate formation, reductase D
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IsfD
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gene name
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IsfD
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isoform, this enzyme represents the major portion of the IsfD activity described for taurine-grown cells
IsfD
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isoform, this enzyme represents the major portion of the IsfD activity described for taurine-grown cells
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IsfD2
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isoform, this enzyme is responsible for the low activity observed in extracts of ammonium-grown cells
IsfD2
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isoform, this enzyme is responsible for the low activity observed in extracts of ammonium-grown cells
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NADPH-dependent sulfoacetaldehyde reductase
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NADPH-dependent sulfoacetaldehyde reductase
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brenda
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brenda
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2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
4-oxobutyrate + NADPH + H+
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additional information
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2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
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ir
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
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ir
4-oxobutyrate + NADPH + H+
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4-oxobutyrate + NADPH + H+
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ir
additional information
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NADH is not a substrate
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additional information
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NADH is not a substrate
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NADPH
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highly specific for NADPH. NADH is not a substrate.
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4-oxobutyrate
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90% substrate inhibition at 20 mM
additional information
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not inhibited by formaldehyde, acetaldehyde, betaine aldehyde, propionaldehyde, DL-glyceraldehyde, phosphonoacetaldehyde, glyoxylate, 2-oxobutyrate, 4-oxobutyrate and 3-sulfopropanaldehyde
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0.13
2-sulfoacetaldehyde
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in 0.02 mMTris/H2SO4 buffer, pH 9.0, at 23°C
0.061
NADPH
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in 0.02 mMTris/H2SO4 buffer, pH 9.0, at 23°C
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6.5 - 9
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IsfD shows a broad pH optimum from about pH 6.5 to pH 9.5. There is a steep increase in activity from pH 4.5 (negligible activity) and an equally steep decrease above pH 9.5
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IsfD is detected at low levels in extracts of ammonium-grown cells
brenda
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IsfD is detected at low levels in extracts of ammonium-grown cells
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brenda
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IsfD is detected at high levels in extracts of taurine-grown cells
brenda
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IsfD is detected at high levels in extracts of taurine-grown cells
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brenda
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27100
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estimated from amino acid sequence
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9
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IsfD is stable in Tris/H2SO4 buffer, pH 9.0
709846
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Mono Q column chromatography, phenyl Superose gel filtration
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Krejcík, Z.; Hollemeyer, K.; Smits, T.H.; Cook, A.M.
Isethionate formation from taurine in Chromohalobacter salexigens: purification of sulfoacetaldehyde reductase
Microbiology
156
1547-1555
2010
Chromohalobacter salexigens, Chromohalobacter salexigens DSM 3043
brenda
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