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

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.17.99.3
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RECOMMENDED NAME
GeneOntology No.
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Primary bile acid biosynthesis
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
119799-47-2
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152787-68-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor
(24R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
show the reaction diagram
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the 25S epimer is a preferential substrate
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?
(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
show the reaction diagram
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-
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?
(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA + H2O + acceptor
(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-en-27-oic acid + reduced acceptor
show the reaction diagram
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no activity with (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
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?
2-methylhexanoyl-CoA + H2O + acceptor
3-hydroxy-2-methylhexanoyl-CoA + reduced acceptor
show the reaction diagram
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?
2-methylpalmitoyl-CoA + H2O + acceptor
3-hydroxy-2-methylhexandecanoyl-CoA + reduced acceptor
show the reaction diagram
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?
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
show the reaction diagram
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conversion of the coenzyme A ester is lower than with the free acid as substrate
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?
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoic acid + reduced acceptor
show the reaction diagram
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?
pristanoyl-CoA + H2O + acceptor
3-hydroxy-1,6,10,14-tetramethylpentadecanoyl-CoA + reduced acceptor
show the reaction diagram
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?
trihydroxycoprostanoyl-CoA + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxycoprostanoyl-CoA + reduced acceptor
show the reaction diagram
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?
additional information
?
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noninducible enzyme
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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noninducible enzyme
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
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marked inhibition of reaction with 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid
FAD
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contains most likely 2 mol of loosely bound FAD per mol of enzyme
FMN
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slight
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA
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palmitoyl-CoA
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additional information
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oxygen may be obligatory since there is almost complete inhibition when the reaction is performed in an atmosphere consisting of nitrogen
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Butanediol
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activates
1,2-propanediol
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activates
1,3-Propanediol
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activates
2,3-Butanediol
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activates
albumin
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required
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ATP
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required
GTP
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stimulates to a lesser degree than ATP
ITP
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stimulates to a lesser degree than ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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pH 6.5: about 30% of maximal activity, pH 8.5: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68800
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2 * 68800, SDS-PAGE
69000
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2 * 69000, SDS-PAGE
120000
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gel filtration
139000
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gel filtration
175000
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non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in presence of dithiothreitol, the enzyme is very stable in high concentrations of ethylene glycol,1,2-propanediol, 1,3-propanediol, 1,2-butanediol, 2,3-butanediol and 1,3-butanediol, 40-60 v/v
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,2-butanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
1,2-propanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
1,3-butanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
1,3-propanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
2,3-butanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
Ethylene glycol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in COS cells