CYP51—the omnipotent P450
Sterol 14α-demethylase (CYP51) is the single cytochrome P450 (CYP) required for sterol biosynthesis in different phyla, and it is the most widely distributed P450 gene family being found in all biological kingdoms. It catalyzes the first step following cyclization in sterol biosynthesis such as remo...
Gespeichert in:
| Veröffentlicht in: | Molecular and cellular endocrinology 2004-02, Vol.215 (1), p.165-170 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 170 |
|---|---|
| container_issue | 1 |
| container_start_page | 165 |
| container_title | Molecular and cellular endocrinology |
| container_volume | 215 |
| creator | Lepesheva, Galina I Waterman, Michael R |
| description | Sterol 14α-demethylase (CYP51) is the single cytochrome P450 (CYP) required for sterol biosynthesis in different phyla, and it is the most widely distributed P450 gene family being found in all biological kingdoms. It catalyzes the first step following cyclization in sterol biosynthesis such as removal of the 14α-methyl group from lanosterol in the cholesterol biosynthetic pathway, leading to formation of the initial substrate in steroid hormone biosynthesis. CYP51 from different phyla have low sequence similarity across kingdoms and contain only about 40 conserved amino acid residues in the whole family. An attempt to predict the possible role of these conserved residues is being made by a combination of the results of site-directed mutagenesis and information from the known crystal structure of sterol 14α-demethylase from
Mycobacterium tuberculosis. |
| doi_str_mv | 10.1016/j.mce.2003.11.016 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_20709412</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0303720703005148</els_id><sourcerecordid>20709412</sourcerecordid><originalsourceid>FETCH-LOGICAL-c380t-5094a62dda9a8f81fe8dbce3a071a69f84498400d22342736e473ec6aab60c843</originalsourceid><addsrcrecordid>eNp9kM1KAzEUhYMotlYfQATpyt2M9yaZSQZXUvyDgl3owlVIM3dwSmemJlOhOx_CJ_RJTGnBnasLh3PO5XyMnSOkCJhfL9LGUcoBRIqYRuWADVErnmjI1CEbggCRKA5qwE5CWACAyrg-ZgPMgOdYwJBdTN5mGf58fffvNO6atl51PbX9eCYzOGVHlV0GOtvfEXu9v3uZPCbT54enye00cUJDn2RQSJvzsrSF1ZXGinQ5dyQsKLR5UWkpCy0BSs6F5ErkJJUgl1s7z8FpKUbsate78t3HmkJvmjo4Wi5tS906mDggvkAejbgzOt-F4KkyK1831m8MgtkSMQsTiZgtEYNoohIzl_vy9byh8i-xRxANNzsDxYmfNXkTXE2to7L25HpTdvU_9b9M0m5W</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20709412</pqid></control><display><type>article</type><title>CYP51—the omnipotent P450</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Lepesheva, Galina I ; Waterman, Michael R</creator><creatorcontrib>Lepesheva, Galina I ; Waterman, Michael R</creatorcontrib><description>Sterol 14α-demethylase (CYP51) is the single cytochrome P450 (CYP) required for sterol biosynthesis in different phyla, and it is the most widely distributed P450 gene family being found in all biological kingdoms. It catalyzes the first step following cyclization in sterol biosynthesis such as removal of the 14α-methyl group from lanosterol in the cholesterol biosynthetic pathway, leading to formation of the initial substrate in steroid hormone biosynthesis. CYP51 from different phyla have low sequence similarity across kingdoms and contain only about 40 conserved amino acid residues in the whole family. An attempt to predict the possible role of these conserved residues is being made by a combination of the results of site-directed mutagenesis and information from the known crystal structure of sterol 14α-demethylase from
Mycobacterium tuberculosis.</description><identifier>ISSN: 0303-7207</identifier><identifier>EISSN: 1872-8057</identifier><identifier>DOI: 10.1016/j.mce.2003.11.016</identifier><identifier>PMID: 15026190</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Amino acid sequence alignment ; Animals ; Cytochrome P-450 Enzyme System - chemistry ; Cytochrome P-450 Enzyme System - physiology ; Cytochrome P450 ; Evolution, Molecular ; Humans ; Mutagenesis, Site-Directed ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - enzymology ; Mycobacterium tuberculosis - genetics ; Oxidation-Reduction ; Oxidoreductases - chemistry ; Oxidoreductases - genetics ; Oxidoreductases - physiology ; Site-directed mutagenesis ; Sterol 14-Demethylase ; Sterol 14α-demethylase ; Sterol biosynthesis</subject><ispartof>Molecular and cellular endocrinology, 2004-02, Vol.215 (1), p.165-170</ispartof><rights>2003 Elsevier Ireland Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-5094a62dda9a8f81fe8dbce3a071a69f84498400d22342736e473ec6aab60c843</citedby><cites>FETCH-LOGICAL-c380t-5094a62dda9a8f81fe8dbce3a071a69f84498400d22342736e473ec6aab60c843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.mce.2003.11.016$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15026190$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lepesheva, Galina I</creatorcontrib><creatorcontrib>Waterman, Michael R</creatorcontrib><title>CYP51—the omnipotent P450</title><title>Molecular and cellular endocrinology</title><addtitle>Mol Cell Endocrinol</addtitle><description>Sterol 14α-demethylase (CYP51) is the single cytochrome P450 (CYP) required for sterol biosynthesis in different phyla, and it is the most widely distributed P450 gene family being found in all biological kingdoms. It catalyzes the first step following cyclization in sterol biosynthesis such as removal of the 14α-methyl group from lanosterol in the cholesterol biosynthetic pathway, leading to formation of the initial substrate in steroid hormone biosynthesis. CYP51 from different phyla have low sequence similarity across kingdoms and contain only about 40 conserved amino acid residues in the whole family. An attempt to predict the possible role of these conserved residues is being made by a combination of the results of site-directed mutagenesis and information from the known crystal structure of sterol 14α-demethylase from
Mycobacterium tuberculosis.</description><subject>Amino acid sequence alignment</subject><subject>Animals</subject><subject>Cytochrome P-450 Enzyme System - chemistry</subject><subject>Cytochrome P-450 Enzyme System - physiology</subject><subject>Cytochrome P450</subject><subject>Evolution, Molecular</subject><subject>Humans</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - enzymology</subject><subject>Mycobacterium tuberculosis - genetics</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - genetics</subject><subject>Oxidoreductases - physiology</subject><subject>Site-directed mutagenesis</subject><subject>Sterol 14-Demethylase</subject><subject>Sterol 14α-demethylase</subject><subject>Sterol biosynthesis</subject><issn>0303-7207</issn><issn>1872-8057</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KAzEUhYMotlYfQATpyt2M9yaZSQZXUvyDgl3owlVIM3dwSmemJlOhOx_CJ_RJTGnBnasLh3PO5XyMnSOkCJhfL9LGUcoBRIqYRuWADVErnmjI1CEbggCRKA5qwE5CWACAyrg-ZgPMgOdYwJBdTN5mGf58fffvNO6atl51PbX9eCYzOGVHlV0GOtvfEXu9v3uZPCbT54enye00cUJDn2RQSJvzsrSF1ZXGinQ5dyQsKLR5UWkpCy0BSs6F5ErkJJUgl1s7z8FpKUbsate78t3HmkJvmjo4Wi5tS906mDggvkAejbgzOt-F4KkyK1831m8MgtkSMQsTiZgtEYNoohIzl_vy9byh8i-xRxANNzsDxYmfNXkTXE2to7L25HpTdvU_9b9M0m5W</recordid><startdate>20040227</startdate><enddate>20040227</enddate><creator>Lepesheva, Galina I</creator><creator>Waterman, Michael R</creator><general>Elsevier Ireland Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>20040227</creationdate><title>CYP51—the omnipotent P450</title><author>Lepesheva, Galina I ; Waterman, Michael R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-5094a62dda9a8f81fe8dbce3a071a69f84498400d22342736e473ec6aab60c843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino acid sequence alignment</topic><topic>Animals</topic><topic>Cytochrome P-450 Enzyme System - chemistry</topic><topic>Cytochrome P-450 Enzyme System - physiology</topic><topic>Cytochrome P450</topic><topic>Evolution, Molecular</topic><topic>Humans</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - enzymology</topic><topic>Mycobacterium tuberculosis - genetics</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - genetics</topic><topic>Oxidoreductases - physiology</topic><topic>Site-directed mutagenesis</topic><topic>Sterol 14-Demethylase</topic><topic>Sterol 14α-demethylase</topic><topic>Sterol biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lepesheva, Galina I</creatorcontrib><creatorcontrib>Waterman, Michael R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Molecular and cellular endocrinology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lepesheva, Galina I</au><au>Waterman, Michael R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CYP51—the omnipotent P450</atitle><jtitle>Molecular and cellular endocrinology</jtitle><addtitle>Mol Cell Endocrinol</addtitle><date>2004-02-27</date><risdate>2004</risdate><volume>215</volume><issue>1</issue><spage>165</spage><epage>170</epage><pages>165-170</pages><issn>0303-7207</issn><eissn>1872-8057</eissn><abstract>Sterol 14α-demethylase (CYP51) is the single cytochrome P450 (CYP) required for sterol biosynthesis in different phyla, and it is the most widely distributed P450 gene family being found in all biological kingdoms. It catalyzes the first step following cyclization in sterol biosynthesis such as removal of the 14α-methyl group from lanosterol in the cholesterol biosynthetic pathway, leading to formation of the initial substrate in steroid hormone biosynthesis. CYP51 from different phyla have low sequence similarity across kingdoms and contain only about 40 conserved amino acid residues in the whole family. An attempt to predict the possible role of these conserved residues is being made by a combination of the results of site-directed mutagenesis and information from the known crystal structure of sterol 14α-demethylase from
Mycobacterium tuberculosis.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>15026190</pmid><doi>10.1016/j.mce.2003.11.016</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0303-7207 |
| ispartof | Molecular and cellular endocrinology, 2004-02, Vol.215 (1), p.165-170 |
| issn | 0303-7207 1872-8057 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_20709412 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino acid sequence alignment Animals Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - physiology Cytochrome P450 Evolution, Molecular Humans Mutagenesis, Site-Directed Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology Mycobacterium tuberculosis - genetics Oxidation-Reduction Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - physiology Site-directed mutagenesis Sterol 14-Demethylase Sterol 14α-demethylase Sterol biosynthesis |
| title | CYP51—the omnipotent P450 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T21%3A45%3A39IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=CYP51%E2%80%94the%20omnipotent%20P450&rft.jtitle=Molecular%20and%20cellular%20endocrinology&rft.au=Lepesheva,%20Galina%20I&rft.date=2004-02-27&rft.volume=215&rft.issue=1&rft.spage=165&rft.epage=170&rft.pages=165-170&rft.issn=0303-7207&rft.eissn=1872-8057&rft_id=info:doi/10.1016/j.mce.2003.11.016&rft_dat=%3Cproquest_cross%3E20709412%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20709412&rft_id=info:pmid/15026190&rft_els_id=S0303720703005148&rfr_iscdi=true |