Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.15.36 - sterol 14alpha-demethylase (ferredoxin) and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WPP9

for references in articles please use BRENDA:EC1.14.15.36
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WPP9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
+
6
reduced ferredoxin [iron-sulfur] cluster
+
6
+
3
=
+
+
6
oxidized ferredoxin [iron-sulfur] cluster
+
4
Synonyms
CYP51, G419_21379, sterol demethylase 450, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sterol demethylase 450
-
CYP51
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
-
-
?
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
show the reaction diagram
-
-
-
?
lanosterol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
4,4-dimethylzymosterol + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
additional information
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
estriol + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
? + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, SDS-PAGE, x * 51400, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team