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Information on EC 1.3.1.71 - DELTA24(241)-sterol reductase
for references in articles please use BRENDA:EC1.3.1.71
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.71 DELTA24(241)-sterol reductase
IUBMB Comments
Acts on a range of steroids with a 24(241)-double bond.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.3.1.71
- brefeldin
- tridemorph
- lamin
- copper
-
schizosaccharomyces
- fenpropimorph
- pombe
- azasterol
showSynonyms
erg4p, c-24(28) reductase, c24(28) reductase, c-24(28) sterol reductase, s-adenosylmethionine:sterol c-24 methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C-24(28) reductase
C-24(28) sterol reductase
-
-
-
-
C24(28) reductase
Erg4p
Erg6
S-adenosylmethionine:sterol C-24 methyltransferase
SAM:SMT
sterol DELTA24(28)-methylene reductase
-
-
-
-
sterol DELTA24(28)-reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
acts on a range of steroids with a 24(241)-double bond
-
ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
24-epi-campesterol, fucosterol, and clionasterol biosynthesis (diatoms), ergosterol biosynthesis I, phytosterol biosynthesis (plants)
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SYSTEMATIC NAME
IUBMB Comments
ergosterol:NADP+ DELTA24(241)-oxidoreductase
Acts on a range of steroids with a 24(241)-double bond.
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CAS REGISTRY NUMBER
COMMENTARY
56467-82-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
-
Substrates: -
Products: trivial name ergosterol
Products: trivial name ergosterol
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
Substrates: step in the biosynthesis of ergosta-5,22-dien-3bta-ol, i.e. brassicasterol, the major sterol compound in Paracoccidioides brasiliensis
Products: -
Products: -
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
Substrates: preferred substrate
Products: -
Products: -
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
Substrates: terminal step in ergosterol biosynthesis, pathway overview, presursor analysis
Products: -
Products: -
?
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
-
Substrates: trivial name ergosterol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme-deficient mutants accumulate ergosta-5,7,22,24(24 1)-tetraen-3beta-ol, ergosta-5,7,24(28)-trien-3beta-ol, ergosta-7,24(28)-dien-3beta-ol, stigmasta-5,7,22,24(28)-tetraenol, stigmasta-5,7,24(28)-trienol, stigmasta-8,24(28)-dienol, and stigmasta-7,24(28)-dienol, while ergosterol and 7-dehydroporiferasterol are absent, in contrary to the wild-type strain, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme-deficient mutants accumulate ergosta-5,7,22,24(24 1)-tetraen-3beta-ol, ergosta-5,7,24(28)-trien-3beta-ol, ergosta-7,24(28)-dien-3beta-ol, stigmasta-5,7,22,24(28)-tetraenol, stigmasta-5,7,24(28)-trienol, stigmasta-8,24(28)-dienol, and stigmasta-7,24(28)-dienol, while ergosterol and 7-dehydroporiferasterol are absent, in contrary to the wild-type strain, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: sterol composition with or without addition of azasterol analogue inhibitors, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme transfers either one or two methyl groups to the C-24 position of the sterol side chain producing both C28 and C29 24-alkylsterols in approximately the same proportions whereas most fungal SAM:SMT transfer only one methyl group to the side chain
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme transfers either one or two methyl groups to the C-24 position of the sterol side chain producing both C28 and C29 24-alkylsterols in approximately the same proportions whereas most fungal SAM:SMT transfer only one methyl group to the side chain
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme transfers either one or two methyl groups to the C-24 position of the sterol side chain producing both C28 and C29 24-alkylsterols in approximately the same proportions whereas most fungal SAM:SMT transfer only one methyl group to the side chain
Products: -
Products: -
?
additional information
?
-
-
Substrates: ergosta-7,22,24(28)-trien-3beta-ol, episterol, and fecosterol are poor substrates, 24,25-dihydro-24-methylene lanosterol is no substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
-
Substrates: -
Products: trivial name ergosterol
Products: trivial name ergosterol
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
Substrates: -
Products: -
Products: -
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
Substrates: step in the biosynthesis of ergosta-5,22-dien-3bta-ol, i.e. brassicasterol, the major sterol compound in Paracoccidioides brasiliensis
Products: -
Products: -
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
Substrates: terminal step in ergosterol biosynthesis, pathway overview, presursor analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme-deficient mutants accumulate ergosta-5,7,22,24(24 1)-tetraen-3beta-ol, ergosta-5,7,24(28)-trien-3beta-ol, ergosta-7,24(28)-dien-3beta-ol, stigmasta-5,7,22,24(28)-tetraenol, stigmasta-5,7,24(28)-trienol, stigmasta-8,24(28)-dienol, and stigmasta-7,24(28)-dienol, while ergosterol and 7-dehydroporiferasterol are absent, in contrary to the wild-type strain, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme-deficient mutants accumulate ergosta-5,7,22,24(24 1)-tetraen-3beta-ol, ergosta-5,7,24(28)-trien-3beta-ol, ergosta-7,24(28)-dien-3beta-ol, stigmasta-5,7,22,24(28)-tetraenol, stigmasta-5,7,24(28)-trienol, stigmasta-8,24(28)-dienol, and stigmasta-7,24(28)-dienol, while ergosterol and 7-dehydroporiferasterol are absent, in contrary to the wild-type strain, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: sterol composition with or without addition of azasterol analogue inhibitors, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20-piperidin-2-yl-5alpha-pregnan-20(R),3beta-diol
-
i.e. AZA-1, inhibits the enzyme and the DELTA24-sterol methyltransferase, leads to accumulation of ergosta-5,7,24(28)-trien-3beta-ol in vivo
22-piperidin-2-yl-5alpha-pregnan-3beta,22(S)-diol
-
i.e. AZA-2, specific inhibition of the enzyme, leads to accumulatin of ergosta-5,7,22,24(28)-tetraen-3beta-ol in vivo
22-piperidin-3-yl-5alpha-pregnan-3beta,22(S)-diol
-
i.e. AZA-3, inhibits the enzyme, major proliferative effect and accumulation of lanosterol in vivo
additional information
-
sterol composition with or without addition of azasterol analogue inhibitors, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00032
-
enzyme activity in 40000 x g microsomal fraction, corresponding to endoplasmic reticulum membranes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
organism in its pathogenic yeast-like phase
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ERG4A_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
471
9
54516
Swiss-Prot
other Location (Reliability: 3)
ERG4B_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
571
9
65267
Swiss-Prot
other Location (Reliability: 5)
ERG4_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
469
8
54837
Swiss-Prot
other Location (Reliability: 2)
ERG4_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
596
8
68354
Swiss-Prot
Mitochondrion (Reliability: 3)
ERG4_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
453
8
52546
Swiss-Prot
other Location (Reliability: 3)
ERG4_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
473
7
56040
Swiss-Prot
other Location (Reliability: 2)
Q4DR82_TRYCC
Trypanosoma cruzi (strain CL Brener)
488
9
57773
TrEMBL
other Location (Reliability: 4)
A4HLA8_LEIBR
500
8
58806
TrEMBL
Mitochondrion (Reliability: 5)
B8ML94_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
573
9
65345
TrEMBL
other Location (Reliability: 3)
A0A8J5BBA3_9ASCO
470
9
54902
TrEMBL
other Location (Reliability: 5)
A0A3R7KUI7_TRYRA
488
7
57663
TrEMBL
Mitochondrion (Reliability: 5)
Q83CC1_COXBU
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
459
9
53730
TrEMBL
-
R9PHU0_PSEHS
Pseudozyma hubeiensis (strain SY62)
761
0
83580
TrEMBL
other Location (Reliability: 3)
A0A3G2S5X5_9BASI
535
8
62388
TrEMBL
Mitochondrion (Reliability: 4)
A0A060THR7_BLAAD
465
7
55021
TrEMBL
other Location (Reliability: 3)
A0A3Q8IM20_LEIDO
496
7
58111
TrEMBL
other Location (Reliability: 5)
A0A088RZI1_9TRYP
500
8
58826
TrEMBL
Mitochondrion (Reliability: 4)
A0A8J5ARN2_9ASCO
470
9
55006
TrEMBL
other Location (Reliability: 4)
A4I8T4_LEIIN
496
7
58111
TrEMBL
other Location (Reliability: 5)
E9B3Q0_LEIMU
Leishmania mexicana (strain MHOM/GT/2001/U1103)
496
8
58343
TrEMBL
Mitochondrion (Reliability: 5)
A0A364NFK3_9PLEO
273
3
29851
TrEMBL
other Location (Reliability: 2)
A0A0F4YQW0_TALEM
549
8
63456
TrEMBL
other Location (Reliability: 4)
A9KFQ8_COXBN
Coxiella burnetii (strain Dugway 5J108-111)
459
9
53730
TrEMBL
-
A0A0F8BMZ7_CERFI
530
9
60866
TrEMBL
other Location (Reliability: 1)
A0A0B7FVI8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
474
9
54474
TrEMBL
other Location (Reliability: 4)
C5P3D8_COCP7
Coccidioides posadasii (strain C735)
569
8
65295
TrEMBL
other Location (Reliability: 4)
Q4DIV5_TRYCC
Trypanosoma cruzi (strain CL Brener)
488
8
57809
TrEMBL
other Location (Reliability: 4)
M5BRQ8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
212
3
25085
TrEMBL
Secretory Pathway (Reliability: 2)
K0KSX4_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
458
8
53819
TrEMBL
other Location (Reliability: 3)
A0A0B7G682_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
472
9
54874
TrEMBL
other Location (Reliability: 5)
B2ZWG1_9STRA
354
0
40851
TrEMBL
other Location (Reliability: 4)
A0A084G7W9_PSEDA
469
8
54339
TrEMBL
other Location (Reliability: 3)
Q4Q4D7_LEIMA
441
7
51714
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8J8W6T8_9EURO
548
9
63330
TrEMBL
other Location (Reliability: 3)
W1QC02_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
474
8
55182
TrEMBL
other Location (Reliability: 3)
A0A3R7LV52_9TRYP
488
8
57384
TrEMBL
Mitochondrion (Reliability: 5)
B9WD50_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
469
8
54891
TrEMBL
other Location (Reliability: 2)
M5CCD3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
459
8
53409
TrEMBL
other Location (Reliability: 5)
A0A0W4ZCX9_PNEC8
Pneumocystis carinii (strain B80)
510
0
60063
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of 3 enzyme-deficient strains resistant to nystatin, analysis of sterol content and spetra in the mutants, overview
additional information
-
construction of 3 enzyme-deficient strains resistant to nystatin, analysis of sterol content and spetra in the mutants, overview
-
additional information
analysis of sterol compositions of wild-type Sacchromyces cerevisiae strain BY4742, the erg6 knockout mutant (DELTAerg6), and DELTAerg6 expressing the Pneumocystis carinii or the Saccharomyces cerevisiae erg6 gene by a variety of chromatographic and spectroscopic procedures. The Pneumocystis carinii SAM:SMT in the DELTAerg6 restores its ability to produce the C28 sterol ergosterol as the major sterol, and also results in low levels of C29 sterols, overview. While the Pneumocystis carinii SAM:SMT in the yeast DELTAerg6 cells is able to transfer a second methyl group to the side chain, the action of DELTA24(28)-sterol reductase (coded by the erg4 gene) in the yeast cells prevents the formation and accumulation of as many C29 sterols as that found in Pneumocystis carinii
additional information
-
analysis of sterol compositions of wild-type Sacchromyces cerevisiae strain BY4742, the erg6 knockout mutant (DELTAerg6), and DELTAerg6 expressing the Pneumocystis carinii or the Saccharomyces cerevisiae erg6 gene by a variety of chromatographic and spectroscopic procedures. The Pneumocystis carinii SAM:SMT in the DELTAerg6 restores its ability to produce the C28 sterol ergosterol as the major sterol, and also results in low levels of C29 sterols, overview. While the Pneumocystis carinii SAM:SMT in the yeast DELTAerg6 cells is able to transfer a second methyl group to the side chain, the action of DELTA24(28)-sterol reductase (coded by the erg4 gene) in the yeast cells prevents the formation and accumulation of as many C29 sterols as that found in Pneumocystis carinii
additional information
-
analysis of sterol compositions of wild-type Sacchromyces cerevisiae strain BY4742, the erg6 knockout mutant (DELTAerg6), and DELTAerg6 expressing the Pneumocystis carinii or the Saccharomyces cerevisiae erg6 gene by a variety of chromatographic and spectroscopic procedures. The Pneumocystis carinii SAM:SMT in the DELTAerg6 restores its ability to produce the C28 sterol ergosterol as the major sterol, and also results in low levels of C29 sterols, overview. While the Pneumocystis carinii SAM:SMT in the yeast DELTAerg6 cells is able to transfer a second methyl group to the side chain, the action of DELTA24(28)-sterol reductase (coded by the erg4 gene) in the yeast cells prevents the formation and accumulation of as many C29 sterols as that found in Pneumocystis carinii
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
25% glycerol and cofactor NADPH or NADH at 1.3 mM stabilize the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, after 24 h: completely stable in presence of NADPH or NADH, 42% remaining activity in presence of 10 mM GSH or 2-mercaptoethanol, 33% remaining activity without additives, after 48 h: 93% remianing activity in prsence of 25% glycerol, 37% with 10% glycerol, and 13% remaining activity without additives
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
combined overexpression with sterol acyltransferase in Saccharomyces cerevisiae strain YEH56(pHXA42)
-
gene erg6, recombinant expression in transgenic Saccharomyces cerevisiae erg6 knockout mutant strain and functional complementation
green fluorescence protein fusion protein expressed in Saccharomyces cerevisiae erg4 mutant
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Neal, W.D.; Parks, L.W.
Sterol 24(28) methylene reductase in Saccharomyces cerevisiae
J. Bacteriol.
129
1375-1378
1977
Saccharomyces cerevisiae
brenda
Pierce, H.D., Jr.; Pierce, A.M.; Srinivasan, R.; Unrau, A.M.; Oehlschlager, A.C.
Azasterol inhibitors in yeast. Inhibition of the 24-methylene sterol DELTA24(28)-reductase and DELTA24-sterol methyltransferase of Saccharomyces cerevisiae by 23-azacholesterol
Biochim. Biophys. Acta
529
429-437
1978
Saccharomyces cerevisiae
brenda
Pierce, A.M.; Unrau, A.M.; Oehlschlager, A.C.; Woods, R.A.
Azasterol inhibitors in yeast. Inhibition of the DELTA24-sterol methyltransferase and the 24-methylene sterol DELTA24(28)-reductase in sterol mutants of Saccharomyces cerevisiae
Can. J. Biochem.
57
201-208
1979
Saccharomyces cerevisiae
brenda
Zweytick, D.; Hrastnik, C.; Kohlwein, S.D.; Daum, G.
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