Steroid 15beta-monooxygenase

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Steroid 15beta-monooxygenase
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EC no. 1.14.15.8
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Steroid 15beta-monooxygenase (EC 1.14.15.8, cytochrome P-450meg, cytochrome P450meg, steroid 15beta-hydroxylase, CYP106A2, BmCYP106A2) is an enzyme with systematic name progesterone,reduced-ferredoxin:oxygen oxidoreductase (15beta-hydroxylating) . [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

progesterone + reduced ferredoxin + O2 15beta-hydroxyprogesterone + oxidized ferredoxin + H2O

The enzyme from Bacillus megaterium hydroxylates a variety of 3-oxo-Delta4-steroids in position 15beta.

Related Research Articles

<span class="mw-page-title-main">Cytochrome P450</span> Class of enzymes

Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Estabrook, Cooper, and Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.

Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.

<span class="mw-page-title-main">Aldosterone synthase</span> Protein-coding gene in the species Homo sapiens

Aldosterone synthase, also called steroid 18-hydroxylase, corticosterone 18-monooxygenase or P450C18, is a steroid hydroxylase cytochrome P450 enzyme involved in the biosynthesis of the mineralocorticoid aldosterone and other steroids. The enzyme catalyzes sequential hydroxylations of the steroid angular methyl group at C18 after initial 11β-hydroxylation. It is encoded by the CYP11B2 gene in humans.

<span class="mw-page-title-main">Cholesterol side-chain cleavage enzyme</span> Mammalian protein found in Homo sapiens

Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an acronym for side-chain cleavage. P450scc is a mitochondrial enzyme that catalyzes conversion of cholesterol to pregnenolone. This is the first reaction in the process of steroidogenesis in all mammalian tissues that specialize in the production of various steroid hormones.

<span class="mw-page-title-main">21-Hydroxylase</span> Human enzyme that hydroxylates steroids

Steroid 21-hydroxylase is an enzyme that hydroxylates steroids at the C21 position and is involved in biosynthesis of aldosterone and cortisol. The enzyme converts progesterone and 17α-hydroxyprogesterone into 11-deoxycorticosterone and 11-deoxycortisol, respectively, within metabolic pathways that ultimately lead to aldosterone and cortisol. Deficiency in the enzyme may cause congenital adrenal hyperplasia.

<span class="mw-page-title-main">Steroid 11β-hydroxylase</span> Protein found in mammals

Steroid 11β-hydroxylase, also known as steroid 11β-monooxygenase, is a steroid hydroxylase found in the zona glomerulosa and zona fasciculata of the adrenal cortex. Named officially the cytochrome P450 11B1, mitochondrial, it is a protein that in humans is encoded by the CYP11B1 gene. The enzyme is involved in the biosynthesis of adrenal corticosteroids by catalyzing the addition of hydroxyl groups during oxidation reactions.

In enzymology, a corticosterone 18-monooxygenase (EC 1.14.15.5) is an enzyme that catalyzes the chemical reaction

Ecdysone 20-monooxygenase (EC 1.14.99.22) is an enzyme that catalyzes the chemical reaction

Alkylglycerol monooxygenase (AGMO) is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipids. This enzyme was first described in 1964 as a pteridine-dependent ether lipid cleaving enzyme. In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7. In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.

In enzymology, a leukotriene-B4 20-monooxygenase (EC 1.14.13.30) is an enzyme that catalyzes the chemical reaction

In enzymology, a steroid 11beta-monooxygenase (EC 1.14.15.4) is an enzyme that catalyzes the chemical reaction

In enzymology, a steroid 17alpha-monooxygenase (EC 1.14.99.9) is an enzyme that catalyzes the chemical reaction

In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Nicotinate dehydrogenase</span> Class of enzymes

In enzymology, a nicotinate dehydrogenase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Adrenal ferredoxin</span> Mammalian protein found in Homo sapiens

Adrenal ferredoxin is a protein that in humans is encoded by the FDX1 gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.

<span class="mw-page-title-main">Adrenodoxin reductase</span> Protein-coding gene in the species Homo sapiens

Adrenodoxin reductase, was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.

<span class="mw-page-title-main">CYP7B1</span> Protein-coding gene in the species Homo sapiens

25-hydroxycholesterol 7-alpha-hydroxylase also known as oxysterol and steroid 7-alpha-hydroxylase is an enzyme that in humans is encoded by the CYP7B1 gene. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids.

Cytochrome P450 BM3 is a Prokaryote Cytochrome P450 enzyme originally from Bacillus megaterium catalyzes the hydroxylation of several long-chain fatty acids at the ω–1 through ω–3 positions. This bacterial enzyme belongs to CYP family CYP102, with the CYP Symbol CYP102A1.This CYP family constitutes a natural fusion between the CYP domain and an NADPH-dependent cytochrome P450 reductase.

Cytochrome P450 family 109 subfamily E member 1 is a prokaryote monooxygenase originally from Bacillus megaterium, could atc as a 24- and 25-Hydroxylase for Cholesterol.

References

  1. Berg A, Ingelman-Sundberg M, Gustafsson JA (June 1979). "Purification and characterization of cytochrome P-450meg". The Journal of Biological Chemistry. 254 (12): 5264–71. doi: 10.1016/S0021-9258(18)50589-5 . PMID   109432.
  2. Berg A, Gustafsson JA, Ingelman-Sundberg M (May 1976). "Characterization of a cytochrome P-450-dependent steroid hydroxylase system present in Bacillus megaterium". The Journal of Biological Chemistry. 251 (9): 2831–8. doi: 10.1016/S0021-9258(17)33564-0 . PMID   177422.
  3. Lisurek M, Kang MJ, Hartmann RW, Bernhardt R (June 2004). "Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry". Biochemical and Biophysical Research Communications. 319 (2): 677–82. doi:10.1016/j.bbrc.2004.05.037. PMID   15178459.
  4. Goñi G, Zöllner A, Lisurek M, Velázquez-Campoy A, Pinto S, Gómez-Moreno C, Hannemann F, Bernhardt R, Medina M (November 2009). "Cyanobacterial electron carrier proteins as electron donors to CYP106A2 from Bacillus megaterium ATCC 13368". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794 (11): 1635–42. doi:10.1016/j.bbapap.2009.07.012. PMID   19635596.
  5. Lisurek M, Simgen B, Antes I, Bernhardt R (June 2008). "Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation". ChemBioChem. 9 (9): 1439–49. doi:10.1002/cbic.200700670. PMID   18481342. S2CID   10667895.