Taurochenodeoxycholate 6α-hydroxylase

A taurochenodeoxycholate 6alpha-hydroxylase (EC 1.14.14.57), (also called taurochenodeoxycholate 6alpha-monooxygenase) is an enzyme with systematic name taurochenodeoxycholate,NADPH:oxygen oxidoreductase (6alpha-hydroxylating). In humans, the multifunction protein CYP3A4 carries out this role among many others, while a separate protein in pigs, CYP4A21, has also been found to catalyze this same reaction.[1][2][3] This enzyme catalyses some hydroxylation reactions of bile acids.[4]

Taurochenodeoxycholate 6alpha-hydroxylase
Identifiers
EC no.1.14.14.57
CAS no.105669-85-0
Databases
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BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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Reactions catalysed

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The bile acid, lithocholic acid, is converted to hyodeoxycholic acid:[5]

 
 
O2 + H+
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
 

The enzyme uses a combination of molecular oxygen and nicotinamide adenine dinucleotide phosphate (NADPH) for the oxidation.

Similarly, taurochenodeoxycholic acid is converted to taurohyocholic acid:[6]

 
 
O2 + H+
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
 

The enzyme is a cytochrome P450 protein containing heme.[7]

See also

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References

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  1. Lundell K, Hansson R, Wikvall K (March 2001). "Cloning and expression of a pig liver taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21): a novel member of the CYP4A subfamily". The Journal of Biological Chemistry. 276 (13): 9606–12. doi:10.1074/jbc.M006584200. PMID 11113117.
  2. Lundell K, Wikvall K (November 2003). "Gene structure of pig sterol 12alpha-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6alpha-hydroxylase (CYP4A21)". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1634 (3): 86–96. doi:10.1016/j.bbalip.2003.09.002. PMID 14643796.
  3. Russell DW (2003). "The enzymes, regulation, and genetics of bile acid synthesis". Annual Review of Biochemistry. 72: 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.
  4. Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C (March 2001). "Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure". The Journal of Biological Chemistry. 276 (10): 7291–301. doi:10.1074/jbc.M006877200. PMID 11069906.
  5. Araya Z, Wikvall K (April 1999). "6alpha-hydroxylation of taurochenodeoxycholic acid and lithocholic acid by CYP3A4 in human liver microsomes". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1438 (1): 47–54. doi:10.1016/s1388-1981(99)00031-1. PMID 10216279.
  6. Araya Z, Hellman U, Hansson R (August 1995). "Characterisation of taurochenodeoxycholic acid 6 alpha-hydroxylase from pig liver microsomes". European Journal of Biochemistry. 231 (3): 855–61. doi:10.1111/j.1432-1033.1995.0855d.x. PMID 7649186.
  7. Enzyme 1.14.14.57 at KEGG Pathway Database.
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