Information on EC 1.14.15.6 - cholesterol monooxygenase (side-chain-cleaving)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.15.6
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RECOMMENDED NAME
GeneOntology No.
cholesterol monooxygenase (side-chain-cleaving)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
show the reaction diagram
(1c)
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(22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
(1b)
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cholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
(1a)
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cholesterol + 6 reduced adrenodoxin + 3 O2 + 6 H+ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
show the reaction diagram
overall reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
androgen and estrogen metabolism
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Steroid hormone biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
cholesterol,reduced-adrenal-ferredoxin:oxygen oxidoreductase (side-chain-cleaving)
A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
37292-81-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
hircus
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
non-breeding male
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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1011323 A+, 1013775 A+, 1139735 A+, 1337861 A+, 1338031 A+, 1338119 A+, 1338171 A+, 1338172 A+, 1338196 A+, 1348817 A+, 1348835 A+, 1348890 A+, 1387881 A+, 1415710 A+, 1443776 A+, 1522031 A+, 1531941 A+, 1587873 A+, 1636860 A+, 1677545 A+, 1677551 A+, 1677760 A+, 1677762 A+, 1677825 A+, 1677827 A+, 1677839 A+, 1677859 A+, 1677867 A+, 1677871 A+, 1677873 A+, 1677877 A+, 1677897 A+, 1677960 A+, 1677970 A+, 1678000 A+, 1678045 A+, 1678083 A+, 1678096 A+, 1678103 A+, 1678110 A+, 1678121 A+, 1678128 A+, 1678151 A+, 1678163 A+, 1678170 A+, 1678178 A+, 1678199 A+, 1678230 A+, 1678276 A+, 1678289 A+, 1678291 A+, 1678313 A+, 1678317 A+, 1678341 A+, 1678343 A+, 1678344 A+, 2129112 A+, 2182383 A+, 2190201 A+, 2195835 A+, 2236693 A+, 2236700 A+, 2236706 A+, 2236755 A+, 2236780 A+, 2249310 A+, 2332292 A+, 2402206 A+, 2470905 A+, 2481885 A+, 2713132 A+, 2745905 A+, 2745949 A+, 2745981 A+, 2745992 A+, 2745994 A+, 2746001 A+, 2746048 A+, 2746059 A+, 2746070 A+, 2746079 A+, 2746084 A+, 2746094 A+, 2746111 A+, 2746153 A+, 392745 A+, 392746 A+, 785715 A+, 785813 A+, 968990 A+, 985294 A+, 985337 A+, 985346 A+, 985369 A+, 985370 A+, 985371 A+, 985526 A+, 985540 A+, 985546 A+, 1001330 A++, 1011065 A++, 1012783 A++, 1012863 A++, 1223326 A++, 1240772 A++, 1254879 A++, 1337617 A++, 1337714 A++, 1348779 A++, 1348812 A++, 1386385 A++, 1635927 A++, 1677393 A++, 1677637 A++, 1677860 A++, 1677901 A++, 1677903 A++, 1677914 A++, 1677915 A++, 1677923 A++, 1677927 A++, 1677935 A++, 1677947 A++, 1677952 A++, 1677993 A++, 1678006 A++, 1678008 A++, 1678015 A++, 1678034 A++, 1678058 A++, 1678064 A++, 1678077 A++, 1678094 A++, 1678108 A++, 1678147 A++, 2236712 A++, 2236719 A++, 2236742 A++, 2236765 A++, 2250442 A++, 2470890 A++, 2658994 A++, 2745957 A++, 2745968 A++, 2746017 A++, 2746045 A++, 2746077 A++, 669941 A++, 687991 A++, 985297 A++, 985304 A++, 985305 A++, 985306 A++, 985326 A++, 985328 A++, 985330 A++, 985333 A++, 985339 A++, 985345 A++, 985355 A++, 985381 A++, 985396 A++, 985397 A++, 985414 A++, 985418 A++, 985425 A++, 985433 A++, 985438 A++, 985439 A++, 985450 A++, 985463 A++, 985465 A++, 985479 A++, 985482 A++, 985496 A++, 985507 A++, 1010938 A++, 1011026 A++, 1011607 A++, 1014669 A++, 1014875 A++, 1019606 A++, 1118808 A++, 1162893 A++, 1222789 A++, 1240564 A++, 1240606 A++, 1240618 A++, 1240717 A++, 1242820 A++, 1254734 A++, 1290658 A++, 1337707 A++, 1337792 A++, 1337885 A++, 1338141 A++, 1338142 A++, 1338163 A++, 1348836 A++, 1348899 A++, 1353143 A++, 1385930 A++, 1386505 A++, 1460398 A++, 1512582 A++, 1587041 A++, 1677424 A++, 1677566 A++, 1677608 A++, 1677831 A++, 1677842 A++, 1677843 A++, 1677848 A++, 1677852 A++, 1677865 A++, 1677875 A++, 1677880 A++, 1677890 A++, 1677909 A++, 1677919 A++, 1677920 A++, 1677924 A++, 1677931 A++, 1677938 A++, 1677954 A++, 1677955 A++, 1677978 A++, 1677996 A++, 1678022 A++, 1678030 A++, 1678044 A++, 1678046 A++, 1678049 A++, 1678073 A++, 1678082 A++, 1678085 A++, 1678086 A++, 1678088 A++, 1678093 A++, 1678115 A++, 1678132 A++, 1678140 A++, 1678198 A++, 1678217 A++, 1678228 A++, 2236666 A++, 2236672 A++, 2236679 A++, 2236686 A++, 2236709 A++, 2236711 A++, 2236724 A++, 2236735 A++, 2236750 A++, 2240579 A++, 2248294 A++, 2250082 A++, 2252485 A++, 2304210 A++, 2384519 A++, 2401056 A++, 2401890 A++, 2408524 A++, 2470919 A++, 2470998 A++, 2515147 A++, 2745593 A++, 2745955 A++, 2745956 A++, 2745967 A++, 2745974 A++, 2745975 A++, 2746009 A++, 2746010 A++, 2746043 A++, 2746064 A++, 2746109 A++, 658811 A++, 659756 A++, 770520 A++, 790107 A++, 985320 A++, 985338 A++, 985428 A++, 985468 A++, 985500 A++, 990520 A++, 725962 A+++, 785809 A+++, 985489 A+++, 985506 A+++, 985519 A+++, 985536 A+++, 785633 A++++, 985295 A++++, 985302 A++++, 985310 A++++, 985312 A++++, 985343 A++++, 985349 A++++, 985352 A++++, 985354 A++++, 985360 A++++, 985390 A++++, 985404 A++++, 985410 A++++, 985480 A++++
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
shark
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Automatic Mining of ENzyme DAta
synthetic construct
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
the active site cavity in CYP11A1 represents a long curved tube that extends from the protein surface to the heme group, the site of catalysis. Shuttling of the sterol intermediates between the active site entrance and the heme group during the three-step reaction. Structural basis of the strict substrate specificity and high catalytic efficiency of the enzyme, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2
pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
show the reaction diagram
(20S)-22-thiacholesterol + reduced adrenodoxin + O2
(20S,22R)-22-thiacholesterol S-oxide + (20S,22S)-22-thiacholesterol S-oxide
show the reaction diagram
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(22R)-sulfoxide preferentially formed by a factor of 4.2 to 1 over (22S)-sulfoxide
?
(22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2
(20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
17,20-dihydroxyvitamin D2 + reduced adrenodoxin + O2
17,20,24-trihydroxyvitamin D2 + oxidized adrenodoxin + O2
show the reaction diagram
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is slowly metabolized
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?
20,23-dihydroxyvitamin D3 + reduced adrenodoxin + O2
17,20,23-trihydroxyvitamin D3 + oxidized adrenodoxin + H2O
show the reaction diagram
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?
20,23-dihydroxyvitamin D3 + reduced adrenodoxin + O2
17alpha,20,23-trihydroxyvitamin D3 + oxidized adrenodoxin + H2O
show the reaction diagram
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?
20-hydroxyvitamin D2 + reduced adrenodoxin + O2
17,20,24-trihydroxyvitamin D2 + oxidized adrenodoxin + O2
show the reaction diagram
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is a better substrate than vitamin D2 itself
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?
20-hydroxyvitamin D3 + reduced adrenodoxin + O2
20,23-dihydroxyvitamin D3 + 17alpha,20,23-trihydroxyvitamin D3 + oxidized adrenodoxin + H2O
show the reaction diagram
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?
20-hydroxyvitamin D3 + reduced adrenodoxin + O2
20,23-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O
show the reaction diagram
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?
20alpha, 22(R)-dihydroxycholesterol + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
show the reaction diagram
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?
20alpha-hydroxycholesterol + reduced adrenodoxin + O2
pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O
show the reaction diagram
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?
20alpha-hydroxycholesterol + reduced adrenodoxin + O2
pregnenolone + oxidized adrenodoxin + H2O
show the reaction diagram
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?
22(R)-hydroxycholesterol + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
show the reaction diagram
22(R)-hydroxycholesterol + reduced adrenodoxin + O2
pregnenolone + oxidized adrenodoxin + H2O
show the reaction diagram
25-hydroxycholesterol + O2 + reduced ferredoxin
pregnenolone + H2O + ferredoxin + 4-hydroxy-4-methylpentanal
show the reaction diagram
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?
25-hydroxycholesterol + reduced adrenodoxin + O2
pregnenolone + oxidized adrenodoxin + H2O
show the reaction diagram
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?
cholesterol + 2 reduced adrenodoxin + O2
(22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
cholesterol + 6 reduced adrenodoxin + 3 O2
pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
show the reaction diagram
cholesterol + 6 reduced adrenodoxin mutant S112W + 3 O2
pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin mutant S112W + 4 H2O
show the reaction diagram
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overall reaction, adrenodoxin mutant S112W gives a 14fold higher catalytic efficiency compared to wild-type adrenodoxin
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?
cholesterol + reduced adrenal ferredoxin + O2
pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin
show the reaction diagram
cholesterol + reduced adrenal ferredoxin + O2
pregnenolone + adrenal ferredoxin + H2O
show the reaction diagram
cholesterol + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
show the reaction diagram
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cholesterol + reduced adrenodoxin + O2
pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O
show the reaction diagram
cholesterol + reduced ferredoxin + O2
pregnenolone + 4-methylpentanal + oxidized ferredoxin
show the reaction diagram
cholesterol sulfate + reduced adrenodoxin + O2
pregnenolone sulfate + 17-hydroxy-pregnenolone + dehydroisoandrosterone sulfate + oxidized adrenodoxin + H2O
show the reaction diagram
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?
vitamin D2 + reduced adrenodoxin + O2
17,20,24-trihydroxyvitamin D2 + oxidized adrenodoxin + H2O
show the reaction diagram
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P450scc catalyzes three sequential hydroxylations of D2 producing 20-hydroxyvitamin D2, 17,20-dihydroxyvitamin D2, and 17,20,24-trihydroxyvitamin D2, which dissociate from the active site of P450scc and accumulate in the reaction mixture
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?
vitamin D3 + reduced adrenodoxin + O2
20-hydroxyvitamin D3 + oxidized adrenodoxin + H2O
show the reaction diagram
additional information
?
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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
(20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2
pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
show the reaction diagram
(22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2
(20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
cholesterol + 2 reduced adrenodoxin + O2
(22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
cholesterol + 6 reduced adrenodoxin + 3 O2
pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
show the reaction diagram
cholesterol + reduced adrenal ferredoxin + O2
pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin
show the reaction diagram
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first and rate-limiting enzyme in adrenal steroidogenesis
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?
cholesterol + reduced adrenal ferredoxin + O2
pregnenolone + adrenal ferredoxin + H2O
show the reaction diagram
cholesterol + reduced ferredoxin + O2
pregnenolone + 4-methylpentanal + oxidized ferredoxin
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adrenodoxin
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cytochrome P450
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Ferredoxin
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Iron
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the enzyme is a cytochrome P450 enzyme
NADPH
reduced adrenal ferredoxin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(20R,S)-20-amino-5-pregnen-3beta-ol
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20-amine derivative, amine is attached closer to the D-ring than in the 22-amine, very weak inhibitor, 0.1 mM causes less than 20% inhibition
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(20S)-22-thiacholesterol
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competitive inhibitor, is converted enzymatically to a more potent inhibitor, the (22S) and (22R) sulfoxides, inhibition by approximately 75% at 0.001 mM, no inactivation in absence of NADPH and O2
(20S,22R)-22-thiacholesterol S-oxide
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competitive versus cholesterol, binds 10times more tightly than (22S) diastereomer, 25% and 44% inhibition at 0.00005 mM and 0.0001 mM, respectively, complete inhibition at 0.001 mM, no substrate for P-450
(20S,22S)-22-thiacholesterol S-oxide
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competitive versus cholesterol, no substrate for P-450
(22R)-22-Aminocholesterol
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completely inhibited by 0.001 mM, affinity toward the P-450scc almost 3fold greater than that for the (22S) form, competitive versus cholesterol, no substrate for P-450
(22S)-22-Aminocholesterol
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not inhibited below 0.001 mM, competitive versus cholesterol, no substrate for P-450
17,20-dihydroxyvitamin D2
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competitive inhibitor
17beta-amino-5-androsten-3beta-ol
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17-amine derivative, amine is attached closer to the D-ring than in the 22-amine, very weak inhibitor, 0.1 mM causes less than 20% inhibition
22-Amino-23,24-bisnor-5-cholen-3beta-ol
22-amino-23,24-bisnor-5alpha-cholen-3beta-ol
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50% inhibition at 0.003 mM
23,24-bisnor-5-cholene-3beta,22-diol
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competitive inhibitor, 40% inhibition at 0.01 mM, 50% at 0.015 mM, resembles the intermediate 22-hydroxycholesterol but acts as an inhibitor rather than serving as a substrate
23-Amino-24-nor-5-cholen-3beta-ol
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23-amine derivative, same steroid ring structure as cholesterol, competitive inhibitor with respect to cholesterol, 50% inhibition at 0.0001 mM, reversible cooperative binding
24-Amino-5-cholen-3beta-ol
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24-amine derivative, amine attached in greater distance from steroid ring, same steroid ring structure as cholesterol, causes a progressive decrease in inhibitory potency, 50% inhibition at 0.0023 mM, reversible noncooperative binding
25-Amino-26,27-bisnor-5-cholesten-3beta-ol
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25-amine derivative, amine attached in greater distance from steroid ring, causes a progressive decrease in inhibitory potency, 50% inhibition at more than 0.1 mM
adrenodoxin
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oxidized form, high affinity to P-450scc, inhibits side chain cleavage by competition with reduced form
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aminogluthetimide
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cholesterol
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inhibition above 0.003 mM, mitochondrial
Cholesterol sulfate
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inhibition above 0.005 mM, mitochondrial
glycerol
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substrate cholesterol, 50% inhibition at 25% glycerol, substrate 22(R)-hydroxycholesterol, 50% inhibition at 44% glycerol, substrate 20alpha-hydroxycholesterol, 50% inhibition at 48% glycerol, substrate 20alpha, 22(R)-dihydroxycholesterol, 50% inhibition at 51% glycerol
methoxychlor
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pesticide of DDT, suicide inhibitor, competitive to cholesterol, substantial irreversible loss of activity, 5% inhibition within 5 min at 0.2 mM, decrease is suppressed by the presence of cholesterol
phosphatidyl choline
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phosphatidyl ethanolamine
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-di-(2'-hexyl-decanoyl)-sn-glycero-3-phosphocholine
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alpha-branched phosphatidylcholine, inclusion in vesicle-reconstituted system, partially in connection with the nonactivator lipids dimyristoyl-/dioleoyl-phosphatidylcholine, efficiency close to cardiolipin
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1,2-di-(2'-octyl-dodecanoyl)-sn-glycero-phosphocholine
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alpha-branched phosphatidylcholine, inclusion in vesicle-reconstituted system, partially in connection with the nonactivator lipids dimyristoyl-/dioleoyl-phosphatidylcholine, efficiency close to cardiolipin
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Brij
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56, 76 and 96
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cardiolipin
Emulgen
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911 and 913
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fatty acid
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C18, natural detergents in DMPC vesicles, stimulation similar to octyl glucoside
glycerol
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5-20% concentration, 20-50% increase of enzyme activity
Lipid
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from adrenal mitochondria accelerates activity
octyl glucoside
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high concentrations of this detergent cause 50% stimulation of cholesterol side-chain-cleavage in large unilamellar vesicles at low cholesterol concentration, 0.01 mM increase the proportion of P-450 bound by cholesterol
Phospholipid
Runx2
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Triton X-100
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effect onto P-450 itself suggested
Tween 20
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0181
17,20-dihydroxyvitamin D2
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in 0.45% cyclodextrin
0.012
20-hydroxyvitamin D2
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in 0.45% cyclodextrin
0.067
20-hydroxyvitamin D3
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in the presence of 0.45% cyclodextrin
0.012
20alpha-hydroxycholesterol
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0.0004 - 0.0012
adrenodoxin
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0.0005 - 1.18
cholesterol
0.0003 - 0.0232
Cholesterol sulfate
0.0175
vitamin D2
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in 0.45% cyclodextrin
0.0296 - 3.67
vitamin D3
additional information
additional information
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decrease in concentration of adrenodoxin reductase causes a decrease in Km-values for cholesterol and adrenodoxin, in mitochondria, cholesterol is near-saturating for enzyme activity due to low and rate-limiting concentration of adrenodoxin reductase present
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.123
20-hydroxyvitamin D3
Bos taurus
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in the presence of 0.45% cyclodextrin
0.05 - 0.5
cholesterol
0.328 - 1.6
vitamin D3
additional information
additional information
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.83
20-hydroxyvitamin D3
Bos taurus
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in the presence of 0.45% cyclodextrin
10258
0.212 - 11.17
cholesterol
189
0.435 - 11.1
vitamin D3
2767
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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for cholesterol and 20alpha-hydroxycholesterol, 75 mM potassium phosphate buffer
7.3
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assay at
7.4
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
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less than 50% of maximal activity below and above range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 42
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tested in different dimyristoyl-phosphatidylcholine vesicles, breaks in activity at 27-30°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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low level
Manually annotated by BRENDA team
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epithelial ovarian carcinoma
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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basophilic cells, exclusively
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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breast cancer cell, expresses both the 55-kDa isoform and the 32-kDa truncated isoform of CYP11A1
Manually annotated by BRENDA team
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expresses the full length 55-kDa isoform of CYP11A1
Manually annotated by BRENDA team
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low level
Manually annotated by BRENDA team
additional information