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Information on EC 1.3.1.71 - DELTA24(241)-sterol reductase
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1.3.1.71 DELTA24(241)-sterol reductaseIUBMB Comments
Acts on a range of steroids with a 24(241)-double bond.
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Word Map
- 1.3.1.71
- carinii
- pneumocystis
- lanosterol
-
opportunistic
- zymosterol
-
human-derived
- fenpropimorph
-
aids-associated
- azasterol
-
protozoan
-
beta-ol
- jiroveci
-
schizosaccharomyces
- copper
- tridemorph
-
delta7
- pombe
-
lamin
The enzyme appears in viruses and cellular organisms
Synonyms
24-methylene sterol 24(28)-reductase, C-24(28) reductase, C-24(28) sterol reductase, C24(28) reductase, DELTA24(28)-sterol methylreductase, Erg4p, Erg6, S-adenosylmethionine:sterol C-24 methyltransferase, SAM:SMT, SMR, 
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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
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ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
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-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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+
-
-
-
?
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+
-
-
-
?
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+
-
-
trivial name ergosterol
?
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+
ergosterol + NADP+
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-
-
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
-
-
-
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
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-
-
-
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
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step in the biosynthesis of ergosta-5,22-dien-3bta-ol, i.e. brassicasterol, the major sterol compound in Paracoccidioides brasiliensis
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-
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
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preferred substrate
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-
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
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terminal step in ergosterol biosynthesis, pathway overview, presursor analysis
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-
?
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
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-
-
?
ergosta-5,7,22-trien-3beta-ol + NADP+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
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-
-
?
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+
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
-
trivial name ergosterol
-
?
additional information
?
-
-
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
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additional information
?
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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
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additional information
?
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sterol composition with or without addition of azasterol analogue inhibitors, overview
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additional information
?
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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
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-
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additional information
?
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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
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additional information
?
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ergosta-7,22,24(28)-trien-3beta-ol, episterol, and fecosterol are poor substrates, 24,25-dihydro-24-methylene lanosterol is no substrate
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-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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+
-
-
-
?
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+
-
-
-
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADP+
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trivial name ergosterol
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
A0A0W4ZCX9
-
-
-
?
ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
ergosterol + NADP+
A0A0W4ZCX9
-
-
-
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
step in the biosynthesis of ergosta-5,22-dien-3bta-ol, i.e. brassicasterol, the major sterol compound in Paracoccidioides brasiliensis
-
-
?
ergosta-5,7,22,24(28)-tetraen-3beta-ol + NADPH
ergosterol + NADP+
-
terminal step in ergosterol biosynthesis, pathway overview, presursor analysis
-
-
?
additional information
?
-
-
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
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-
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additional information
?
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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
-
-
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additional information
?
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-
sterol composition with or without addition of azasterol analogue inhibitors, overview
-
-
-
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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
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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
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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
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organism in its pathogenic yeast-like phase
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ERG4_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
473
7
56040
Swiss-Prot
STS1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
453
8
52546
Swiss-Prot
K0KSX4_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
458
8
53819
TrEMBL
E9B3Q0_LEIMU
Leishmania mexicana (strain MHOM/GT/2001/U1103)
496
8
58343
TrEMBL
Q83CC1_COXBU
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
459
9
53730
TrEMBL
A0A0B7G682_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
472
9
54874
TrEMBL
M5CCD3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
459
8
53409
TrEMBL
A0A0B7FVI8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
474
9
54474
TrEMBL
W1QC02_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
474
8
55182
TrEMBL
A0A0F8BMZ7_CERFI
530
9
60866
TrEMBL
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
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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.
Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, Erg4p, from the yeast Saccharomyces cerevisiae
FEBS Lett.
470
83-87
2000
Saccharomyces cerevisiae
brenda
Visbal, G.; Alvarez, A.; Moreno, B.; San-Blas, G.
S-adenosyl-L-methionine inhibitors DELTA24-sterol methyltransferase and DELTA24(28)-sterol methylreductase as possible agents against Paracoccidioides brasiliensis
Antimicrob. Agents Chemother.
47
2966-2970
2003
Paracoccidioides brasiliensis
brenda
Jarman, T.R.; Gunatilaka, A.A.L.; Widdowson, D.A.
Biosynthesis of steroids and terpenoids. XI. 24-Methylene sterol 24(28)-reductase of Saccharomyces cerevisiae
Bioorg. Chem.
4
202-211
1975
Saccharomyces cerevisiae
-
brenda
Salimova, E.; Boschetti, A.; Eichenberger, W.; Lutova, L.
Sterol mutants of Chlamydomonas reinhardtii: characterization of three strains deficient in C24(28) reductase
Plant Physiol. Biochem.
37
241-249
1999
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii arg7cw15
-
brenda
He, X.; Guo, X.; Liu, N.; Zhang, B.
Ergosterol production from molasses by genetically modified Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
75
55-60
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae YEH56(pHXA42)
brenda
Kaneshiro, E.; Johnston, L.; Nkinin, S.; Romero, B.; Giner, J.
Sterols of Saccharomyces cerevisiae erg6 knockout mutant expressing the Pneumocystis carinii S-adenosylmethioninesterol C-24 methyltransferase (SAMSMT)
J. Eukaryot. Microbiol.
62
298-306
2015
Pneumocystis carinii (A0A0W4ZCX9), Pneumocystis carinii, Pneumocystis carinii B80 (A0A0W4ZCX9)
brenda
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