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EC Tree
IUBMB Comments A cytochrome P-450 (heme-thiolate) protein found in several bacterial species. The enzyme, which is involved in sterol biosynthesis, catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. The enzyme from Methylococcus capsulatus is fused to the ferredoxin by an alanine-rich linker. cf. EC 1.14.14.154, sterol 14alpha-demethylase.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
6
reduced ferredoxin [iron-sulfur] cluster
+
6
+
3
=
+
+
6
oxidized ferredoxin [iron-sulfur] cluster
+
4
Synonyms
CYP51 ,
G419_21379 , sterol demethylase 450,
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CYP51
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G419_21379
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sterol demethylase 450
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a 14alpha-formylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a DELTA14-steroid + formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1c)
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-
a 14alpha-hydroxymethylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a 14alpha-formylsteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1b)
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a 14alpha-methylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a 14alpha-hydroxymethylsteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1a)
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-
a 14alpha-methylsteroid + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 = a DELTA14-steroid + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
overall reaction
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-
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sterol,reduced ferredoxin:oxygen oxidoreductase (14-methyl cleaving)
A cytochrome P-450 (heme-thiolate) protein found in several bacterial species. The enzyme, which is involved in sterol biosynthesis, catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. The enzyme from Methylococcus capsulatus is fused to the ferredoxin by an alanine-rich linker. cf. EC 1.14.14.154, sterol 14alpha-demethylase.
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24,25-dihydrolanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethyl-5alpha-cholesta-8,14-diene-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
hydroxylanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
oxolanosterol + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
lanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylanosterol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
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-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
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activity depends on presence of natural fusion protein ferredoxin
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?
obtusifoliol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
oxolanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
4,4-dimethylzymosterol + formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
additional information
?
-
24,25-dihydrolanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethyl-5alpha-cholesta-8,14-diene-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
24,25-dihydrolanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethyl-5alpha-cholesta-8,14-diene-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
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-
?
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
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-
?
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
hydroxylanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
oxolanosterol + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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-
?
hydroxylanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
oxolanosterol + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
lanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylanosterol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
?
lanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
hydroxylanosterol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
obtusifoliol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
obtusifoliol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
?
oxolanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
4,4-dimethylzymosterol + formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
oxolanosterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
4,4-dimethylzymosterol + formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
additional information
?
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both flavodoxin and ferredoxin redox systems are able to support the enzymatic activity. Substrates require a 14alpha methyl group and a 8,9 C-C double bond
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?
additional information
?
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both flavodoxin and ferredoxin redox systems are able to support the enzymatic activity. Substrates require a 14alpha methyl group and a 8,9 C-C double bond
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?
additional information
?
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exogenous electron donor systems, Fdx-FdR i.e. Acinetobacter sp. OC4 ferredoxin and ferredoxin reductase, Fld-FdR2 i.e. Escherichia coli flavodoxin and flavodoxin reductase, and Nocardia farcinica iron-sulfur containing NADPH-P450 reductase NfFdR can be used. Fdx-FdR is the most efficient electron donor
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?
additional information
?
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exogenous electron donor systems, Fdx-FdR i.e. Acinetobacter sp. OC4 ferredoxin and ferredoxin reductase, Fld-FdR2 i.e. Escherichia coli flavodoxin and flavodoxin reductase, and Nocardia farcinica iron-sulfur containing NADPH-P450 reductase NfFdR can be used. Fdx-FdR is the most efficient electron donor
-
?
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estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
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-
-
?
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?
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heme
heme-iron reduction is the rate limiting step in catalysis. Protonation of the cysteinate ligand to the ferrous CYP51 underlies the collapse of the Fe(II)-CO adduct of the enzyme from its P450 to its P420 form. The protonation is reversible and the rate of P420 formation is substantially retarded in the estriol-bound form of CYP51
cytochrome P450
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the oxidized absolute spectrum of the purified CYP51, in the absence of substrate, shows a Soret band at 417 nm and alpha-, beta-, and delta-bands at 569, 535, and 369 nm
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cytochrome P450
the oxidized absolute spectrum of the purified enzyme, in the absence of substrate, shows a Soret band at 417 nm and alpha-,beta-, and delta bands at 569, 535, and 369 nm
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Iron
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3.9 molecules per enzyme molecule, 3Fe-4S center of ferredoxin component, one iron molecule bound to heme
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0.0103 - 0.0125
lanosterol
0.0103
lanosterol
FprD fusion construct F1, pH 7.0, temperature not specified in the publication
0.0122
lanosterol
wild-type, pH 7.0, temperature not specified in the publication
0.0125
lanosterol
FprD fusion construct F2, pH 7.0, temperature not specified in the publication
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0.67
lanosterol
wild-type, pH 7.0, temperature not specified in the publication
16.7
lanosterol
FprD fusion construct F1, pH 7.0, temperature not specified in the publication
21.9
lanosterol
FprD fusion construct F2, pH 7.0, temperature not specified in the publication
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50.5
lanosterol
wild-type, pH 7.0, temperature not specified in the publication
1615
lanosterol
FprD fusion construct F1, pH 7.0, temperature not specified in the publication
1763
lanosterol
FprD fusion construct F2, pH 7.0, temperature not specified in the publication
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natural fusion protein of enzyme and ferredoxin
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Uniprot
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Uniprot
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UniProt
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UniProt
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UniProt
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UniProt
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physiological function
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the protein binds azole antifungals with high affinity and the rank order based on affinity matches the ranked order for microbiological sensitivity of the organism
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M2UZT3_9NOCA
474
0
53016
TrEMBL
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CP51_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
451
0
50878
Swiss-Prot
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Q5YWK5_NOCFA
Nocardia farcinica (strain IFM 10152)
452
0
50999
TrEMBL
-
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62000
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x * 62000, SDS-PAGE, recombinant enzyme
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dodecamer
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x * 62000, SDS-PAGE, recombinant enzyme
?
x * 50000, SDS-PAGE, x * 51400, calculated from sequence
?
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x * 50000, SDS-PAGE, x * 51400, calculated from sequence
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homoology modeling of structure
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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synthesis
construction of an artificial self-sufficient cytochrome P450 monooxygenase by fusion of NADPH-P450 reductase FprD, CYP51, and iron-sulfur containing FprD. CYP51-FprD fusion enzymes F1 and F2 in recombinant Escherichia coli catalyze demethylation of lanosterol more efficiently, with kcat/Km values about 35fold higher compared to those of CYP51 and FprD alone
synthesis
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construction of an artificial self-sufficient cytochrome P450 monooxygenase by fusion of NADPH-P450 reductase FprD, CYP51, and iron-sulfur containing FprD. CYP51-FprD fusion enzymes F1 and F2 in recombinant Escherichia coli catalyze demethylation of lanosterol more efficiently, with kcat/Km values about 35fold higher compared to those of CYP51 and FprD alone
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Jackson, C.J.; Lamb, D.C.; Marczylo, T.H.; Warrilow, A.G.; Manning, N.J.; Lowe, D.J.; Kelly, D.E.; Kelly, S.L.
A novel sterol 14alpha-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily
J. Biol. Chem.
277
46959-46965
2002
Methylococcus capsulatus
brenda
Ke, X.; Ding, G.; Ma, B.; Liu, Z.; Zhang, J.; Zheng, Y.
Characterization of a novel CYP51 from Rhodococcus triatomae and its NADH-ferredoxin reductase-coupled application in lanosterol 14alpha-demethylation
Process Biochem.
62
59-68
2017
Rhodococcus triatomae (M2UZT3), Rhodococcus triatomae BKS 15-14 (M2UZT3)
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Jackson, C.J.; Lamb, D.C.; Marczylo, T.H.; Parker, J.E.; Manning, N.L.; Kelly, D.E.; Kelly, S.L.
Conservation and cloning of CYP51 a sterol 14 alpha-demethylase from Mycobacterium smegmatis
Biochem. Biophys. Res. Commun.
301
558-563
2003
Mycolicibacterium smegmatis
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McLean, K.J.; Warman, A.J.; Seward, H.E.; Marshall, K.R.; Girvan, H.M.; Cheesman, M.R.; Waterman, M.R.; Munro, A.W.
Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions
Biochemistry
45
8427-8443
2006
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis H37Rv (P9WPP9)
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Choi, K.Y.; Jung, E.O.; Jung, D.H.; Pandey, B.P.; Lee, N.; Yun, H.; Park, H.Y.; Kim, B.G.
Novel iron-sulfur containing NADPH-reductase from Nocardia farcinica IFM10152 and fusion construction with CYP51 lanosterol demethylase
Biotechnol. Bioeng.
109
630-636
2012
Nocardia farcinica (Q5YWK5), Nocardia farcinica IFM 10152 (Q5YWK5)
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Bellamine, A.; Mangla, A.T.; Nes, W.D.; Waterman, M.R.
Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis
Proc. Natl. Acad. Sci. USA
96
8937-8942
1999
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis H37Rv (P9WPP9)
brenda
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Enzyme Nomenclature
1.14.15.36 sterol 14alpha-demethylase (ferredoxin)
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