1.17.99.3: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase

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For detailed information about 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase, go to the full flat file.

Reaction

Synonyms

3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, THC-CoA oxidase, THCA-CoA oxidase, THCCox, Trihydroxycoprostanoyl-CoA oxidase

ECTree

     1 Oxidoreductases

         1.17 Acting on CH or CH₂ groups

             1.17.99 With unknown physiological acceptors

                1.17.99.3 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase

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8	Activating Compound
6	AA Sequence
2	CAS Registry Number
2	Cloned(Commentary)
3	Cofactor
1	General Stability
3	Inhibitors
8	Localization
5	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
6	Organic Solvent Stability
12	Organism
2	Pathway
1	pH Optimum
1	pH Range
1	pI Value
3	Purification (Commentary)
1	Reaction
6	Reaction Type
12	Reference
11	Source Tissue
2	Specific Activity [micromol/min/mg]
10	Substrates and Products (Substrate)
2	Subunits
15	Synonyms
1	Systematic Name

Systematic Name

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Systematic Name on EC 1.17.99.3 - 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase

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SYSTEMATIC NAME

IUBMB Comments

(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:acceptor 24-oxidoreductase (24R-hydroxylating)

Requires ATP. The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration [1]. However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate and not via hydration of a 24(25) double bond [5]. In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate [1].