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(Redirected from Cholate-CoA ligase)
Cholate—CoA ligase
Identifiers
EC no. 6.2.1.7
CAS no. 9027-90-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Cholate—CoA ligase ( EC 6.2.1.7, BAL, bile acid CoA ligase, bile acid coenzyme A ligase, choloyl-CoA synthetase, choloyl coenzyme A synthetase, cholic thiokinase, cholate thiokinase, cholic acid:CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase, THCA-CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate—CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase (AMP-forming), cholyl-CoA synthetase, trihydroxycoprostanoyl-CoA synthetase) is an enzyme with systematic name cholate:CoA ligase (AMP-forming). [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

(1) ATP + cholate + CoA AMP + diphosphate + choloyl-CoA
(2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA

This enzyme requires Mg2+ for activity.

References

  1. ^ Elliott WH (March 1956). "The enzymic activation of cholic acid by guinea-pig-liver microsomes". The Biochemical Journal. 62 (3): 427–33. PMC  1215932. PMID  13303991.
  2. ^ Elliott WH (February 1957). "The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes". The Biochemical Journal. 65 (2): 315–21. PMC  1199872. PMID  13403911.
  3. ^ Prydz K, Kase BF, Björkhem I, Pedersen JI (August 1988). "Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997–1004. PMID  3183523.
  4. ^ Schepers L, Casteels M, Verheyden K, Parmentier G, Asselberghs S, Eyssen HJ, Mannaerts GP (January 1989). "Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver". The Biochemical Journal. 257 (1): 221–9. PMC  1135559. PMID  2521999.
  5. ^ Mallonee DH, Adams JL, Hylemon PB (April 1992). "The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase". Journal of Bacteriology. 174 (7): 2065–71. PMC  205821. PMID  1551828.
  6. ^ Wheeler JB, Shaw DR, Barnes S (December 1997). "Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes". Archives of Biochemistry and Biophysics. 348 (1): 15–24. doi: 10.1006/abbi.1997.0391. PMID  9390170.
  7. ^ Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S (December 2002). "Molecular cloning and expression of rat liver bile acid CoA ligase". Journal of Lipid Research. 43 (12): 2062–71. doi: 10.1194/jlr.M200260-JLR200. PMID  12454267.

External links

From Wikipedia, the free encyclopedia
(Redirected from Cholate-CoA ligase)
Cholate—CoA ligase
Identifiers
EC no. 6.2.1.7
CAS no. 9027-90-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Cholate—CoA ligase ( EC 6.2.1.7, BAL, bile acid CoA ligase, bile acid coenzyme A ligase, choloyl-CoA synthetase, choloyl coenzyme A synthetase, cholic thiokinase, cholate thiokinase, cholic acid:CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase, THCA-CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate—CoA ligase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase (AMP-forming), cholyl-CoA synthetase, trihydroxycoprostanoyl-CoA synthetase) is an enzyme with systematic name cholate:CoA ligase (AMP-forming). [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

(1) ATP + cholate + CoA AMP + diphosphate + choloyl-CoA
(2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA

This enzyme requires Mg2+ for activity.

References

  1. ^ Elliott WH (March 1956). "The enzymic activation of cholic acid by guinea-pig-liver microsomes". The Biochemical Journal. 62 (3): 427–33. PMC  1215932. PMID  13303991.
  2. ^ Elliott WH (February 1957). "The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes". The Biochemical Journal. 65 (2): 315–21. PMC  1199872. PMID  13403911.
  3. ^ Prydz K, Kase BF, Björkhem I, Pedersen JI (August 1988). "Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997–1004. PMID  3183523.
  4. ^ Schepers L, Casteels M, Verheyden K, Parmentier G, Asselberghs S, Eyssen HJ, Mannaerts GP (January 1989). "Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver". The Biochemical Journal. 257 (1): 221–9. PMC  1135559. PMID  2521999.
  5. ^ Mallonee DH, Adams JL, Hylemon PB (April 1992). "The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase". Journal of Bacteriology. 174 (7): 2065–71. PMC  205821. PMID  1551828.
  6. ^ Wheeler JB, Shaw DR, Barnes S (December 1997). "Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes". Archives of Biochemistry and Biophysics. 348 (1): 15–24. doi: 10.1006/abbi.1997.0391. PMID  9390170.
  7. ^ Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S (December 2002). "Molecular cloning and expression of rat liver bile acid CoA ligase". Journal of Lipid Research. 43 (12): 2062–71. doi: 10.1194/jlr.M200260-JLR200. PMID  12454267.

External links


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