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IUBMB CommentsAlso acts on other 3α-hydroxysteroids with an acidic side-chain. cf. EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Escherichia sp.
Synonyms
alpha-hydroxy-cholanate dehydrogenase, dehydrogenase, 3alpha-hydroxycholanate, more
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alpha-hydroxy-cholanate dehydrogenase
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dehydrogenase, 3alpha-hydroxycholanate
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lithocholate + NAD+ = 3-oxo-5beta-cholan-24-oate + NADH + H+
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MetaCyc
bile acid 7alpha-dehydroxylation, bile acid 7beta-dehydroxylation, bile acids 3-O-epimerization, iso-bile acids biosynthesis I
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lithocholate:NAD+ 3-oxidoreductase
Also acts on other 3alpha-hydroxysteroids with an acidic side-chain. cf. EC 1.1.1.392, 3alpha-hydroxycholanate dehydrogenase (NADP+).
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3alpha-hydroxy-5beta-cholanate + NAD+
3-oxo-5beta-cholanate + NADH
3alpha-hydroxy-bis-norcholanic acid + NAD+
3-oxo-bis-norcholanic acid + NADH
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Substrates: oxidation at the same rate as hydroxycholanic acid
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3alpha-hydroxy-norcholanic acid + NAD+
3-oxo-norcholanic acid + NADH
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Substrates: oxidation at the same rate as hydroxycholanic acid
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cholic acid + NAD+
7alpha,12alpha-dihydroxy-3-oxo-5beta-cholan-24-oic acid + NADH
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Substrates: oxidation at the same rate as hydroxycholanic acid
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dehydrocholic acid + NADH
3-hydroxy-7,12-dihydroxy-5beta-cholan-24-oic acid + NAD+
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Substrates: i.e. 3,7,12-trioxocholan-24-oic acid
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deoxycholic acid + NAD+
12alpha-hydroxy-3-oxo-5beta-cholan-24-oic acid + NADH + H+
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Substrates: oxidation at the same rate as hydroxycholanic acid
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additional information
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Substrates: no substrates: androsterone and tetrahydrocortisone, methylation of carboxyl group or reduction to alcohol inactivates
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3alpha-hydroxy-5beta-cholanate + NAD+

3-oxo-5beta-cholanate + NADH
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Substrates: i.e. lithocholic acid
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3alpha-hydroxy-5beta-cholanate + NAD+
3-oxo-5beta-cholanate + NADH
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Substrates: -
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3alpha-hydroxy-5beta-cholanate + NAD+
3-oxo-5beta-cholanate + NADH
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Substrates: -
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NAD+
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NADP+ cannot replace NAD+
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additional information
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SH-groups are required for activity
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10.4
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oxidation, assay at
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additional information
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oxidation proceeds at alkaline and reduction favorably at neutral pH-values
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tentative identification: E. freundii
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brenda
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brenda
Highest Expressing Human Cell Lines
Cell Line Links
Gene Links
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AK1C2_HUMAN
323
0
36735
Swiss-Prot
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Hayaishi, O.; Saito, Y.; Jakoby, W.B.; Stohlman, E.F.
Reversible enzymatic oxidation of bile acids
Arch. Biochem. Biophys.
56
554-555
1955
Escherichia sp.
brenda
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