Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose
UDP-galactopyranose mutase (UGM) catalyzes the isomerization of UDP-galactopyranose (UDP-Gal p) into UDP-galactofuranose (UDP-Gal f), an essential step of the mycobacterial cell wall biosynthesis. UDP-(6-deoxy-6-fluoro)- d-galactofuranose 1 was tested as substrate of UGM. Turnover could be observed...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2009-02, Vol.19 (3), p.814-816 |
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| creator | Eppe, Guillaume Peltier, Pauline Daniellou, Richard Nugier-Chauvin, Caroline Ferrières, Vincent Vincent, Stéphane P. |
| description | UDP-galactopyranose mutase (UGM) catalyzes the isomerization of UDP-galactopyranose (UDP-Gal
p) into UDP-galactofuranose (UDP-Gal
f), an essential step of the mycobacterial cell wall biosynthesis. UDP-(6-deoxy-6-fluoro)-
d-galactofuranose
1 was tested as substrate of UGM. Turnover could be observed by HPLC. The
k
cat (7.4
s
−1) and the
K
m (24
mM) of
1 were thus measured and compared with those of UDP-Gal
f and other fluorinated analogs. The presence of the fluorine atom at the 6-position had a moderate effect on the rate of the reaction but a huge one on the interactions between the enzyme and its substrate. This result demonstrated that key interactions occur at the vicinity of the 6-position of UDP-galactose in the Michaelis complex. |
| doi_str_mv | 10.1016/j.bmcl.2008.12.014 |
| format | Article |
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p) into UDP-galactofuranose (UDP-Gal
f), an essential step of the mycobacterial cell wall biosynthesis. UDP-(6-deoxy-6-fluoro)-
d-galactofuranose
1 was tested as substrate of UGM. Turnover could be observed by HPLC. The
k
cat (7.4
s
−1) and the
K
m (24
mM) of
1 were thus measured and compared with those of UDP-Gal
f and other fluorinated analogs. The presence of the fluorine atom at the 6-position had a moderate effect on the rate of the reaction but a huge one on the interactions between the enzyme and its substrate. This result demonstrated that key interactions occur at the vicinity of the 6-position of UDP-galactose in the Michaelis complex.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2008.12.014</identifier><identifier>PMID: 19119008</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Analytical, structural and metabolic biochemistry ; Antibacterial agents ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Biological and medical sciences ; Carbohydrate ; Carbohydrates - chemistry ; Catalysis ; Cell Wall - metabolism ; Chemical Sciences ; Chemistry, Pharmaceutical - methods ; Chromatography, High Pressure Liquid ; Conformation ; Drug Design ; Enzymes ; Enzymes and enzyme inhibitors ; Fluorine ; Fluorine - chemistry ; Fundamental and applied biological sciences. Psychology ; Furans - chemistry ; Galactofuranose ; Galactose - analogs & derivatives ; Galactose - chemistry ; Intramolecular Transferases - chemistry ; Isomerases ; Kinetics ; Mechanism ; Medical sciences ; Molecular Conformation ; Mycobacterium ; Mycobacterium - metabolism ; Organic chemistry ; Pharmacology. Drug treatments ; Protein Binding ; Tuberculosis ; Uridine Diphosphate - analogs & derivatives ; Uridine Diphosphate - chemistry</subject><ispartof>Bioorganic & medicinal chemistry letters, 2009-02, Vol.19 (3), p.814-816</ispartof><rights>2009 Elsevier Ltd</rights><rights>2009 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-b21c1ebee9b5dc4b62366a854819a8883286490e3d60b1ef745ba6f5f0c05d1d3</citedby><cites>FETCH-LOGICAL-c450t-b21c1ebee9b5dc4b62366a854819a8883286490e3d60b1ef745ba6f5f0c05d1d3</cites><orcidid>0000-0002-2780-7774 ; 0000-0001-7296-3736</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmcl.2008.12.014$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21123425$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19119008$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00405250$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Eppe, Guillaume</creatorcontrib><creatorcontrib>Peltier, Pauline</creatorcontrib><creatorcontrib>Daniellou, Richard</creatorcontrib><creatorcontrib>Nugier-Chauvin, Caroline</creatorcontrib><creatorcontrib>Ferrières, Vincent</creatorcontrib><creatorcontrib>Vincent, Stéphane P.</creatorcontrib><title>Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>UDP-galactopyranose mutase (UGM) catalyzes the isomerization of UDP-galactopyranose (UDP-Gal
p) into UDP-galactofuranose (UDP-Gal
f), an essential step of the mycobacterial cell wall biosynthesis. UDP-(6-deoxy-6-fluoro)-
d-galactofuranose
1 was tested as substrate of UGM. Turnover could be observed by HPLC. The
k
cat (7.4
s
−1) and the
K
m (24
mM) of
1 were thus measured and compared with those of UDP-Gal
f and other fluorinated analogs. The presence of the fluorine atom at the 6-position had a moderate effect on the rate of the reaction but a huge one on the interactions between the enzyme and its substrate. This result demonstrated that key interactions occur at the vicinity of the 6-position of UDP-galactose in the Michaelis complex.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Antibacterial agents</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate</subject><subject>Carbohydrates - chemistry</subject><subject>Catalysis</subject><subject>Cell Wall - metabolism</subject><subject>Chemical Sciences</subject><subject>Chemistry, Pharmaceutical - methods</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Conformation</subject><subject>Drug Design</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fluorine</subject><subject>Fluorine - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Furans - chemistry</subject><subject>Galactofuranose</subject><subject>Galactose - analogs & derivatives</subject><subject>Galactose - chemistry</subject><subject>Intramolecular Transferases - chemistry</subject><subject>Isomerases</subject><subject>Kinetics</subject><subject>Mechanism</subject><subject>Medical sciences</subject><subject>Molecular Conformation</subject><subject>Mycobacterium</subject><subject>Mycobacterium - metabolism</subject><subject>Organic chemistry</subject><subject>Pharmacology. Drug treatments</subject><subject>Protein Binding</subject><subject>Tuberculosis</subject><subject>Uridine Diphosphate - analogs & derivatives</subject><subject>Uridine Diphosphate - chemistry</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1v1DAQhi0EokvhD3BAuQDikDD-iDdBXFblo0gr0QOVuFm2Y7dekji1nUo98N9xlKVw6mnk8TMzr94XoZcYKgyYvz9UatB9RQCaCpMKMHuENphxVlIG9WO0gZZD2bTs5wl6FuMBMgGMPUUnuMW4zWMb9PsieOXGq-Ly00V5JXupk5_ughx9NMUwJ5lL_u8WZPL6l0kfil3RBTnI5HRhrDU6FX4s4qxicmlOLj-8LdK1KXg5-ej-dv67YOf1wnP0xMo-mhfHeoouv3z-cXZe7r9__Xa225ea1ZBKRbDGRhnTqrrTTHFCOZdNzRrcyqZpKGk4a8HQjoPCxm5ZrSS3tQUNdYc7eorerXuvZS-m4AYZ7oSXTpzv9mLpAWTHSA23OLNvV3YK_mY2MYnBRW36Xo7Gz1FsKeUUb6HO5JsHSQKUEt42GSQrqIOPMRh7rwGDWKIUB7FEKZYoBSYiB5WHXh23z2ow3b-RY3YZeH0EZNSyt9lS7eI9RzAmlJFF5seVM9nhW2eCiNqZUZvOhRye6Lx7SMcfzxi8Xg</recordid><startdate>20090201</startdate><enddate>20090201</enddate><creator>Eppe, Guillaume</creator><creator>Peltier, Pauline</creator><creator>Daniellou, Richard</creator><creator>Nugier-Chauvin, Caroline</creator><creator>Ferrières, Vincent</creator><creator>Vincent, Stéphane P.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><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>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-2780-7774</orcidid><orcidid>https://orcid.org/0000-0001-7296-3736</orcidid></search><sort><creationdate>20090201</creationdate><title>Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose</title><author>Eppe, Guillaume ; Peltier, Pauline ; Daniellou, Richard ; Nugier-Chauvin, Caroline ; Ferrières, Vincent ; Vincent, Stéphane P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-b21c1ebee9b5dc4b62366a854819a8883286490e3d60b1ef745ba6f5f0c05d1d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Antibacterial agents</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate</topic><topic>Carbohydrates - chemistry</topic><topic>Catalysis</topic><topic>Cell Wall - metabolism</topic><topic>Chemical Sciences</topic><topic>Chemistry, Pharmaceutical - methods</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Conformation</topic><topic>Drug Design</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fluorine</topic><topic>Fluorine - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Furans - chemistry</topic><topic>Galactofuranose</topic><topic>Galactose - analogs & derivatives</topic><topic>Galactose - chemistry</topic><topic>Intramolecular Transferases - chemistry</topic><topic>Isomerases</topic><topic>Kinetics</topic><topic>Mechanism</topic><topic>Medical sciences</topic><topic>Molecular Conformation</topic><topic>Mycobacterium</topic><topic>Mycobacterium - metabolism</topic><topic>Organic chemistry</topic><topic>Pharmacology. Drug treatments</topic><topic>Protein Binding</topic><topic>Tuberculosis</topic><topic>Uridine Diphosphate - analogs & derivatives</topic><topic>Uridine Diphosphate - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eppe, Guillaume</creatorcontrib><creatorcontrib>Peltier, Pauline</creatorcontrib><creatorcontrib>Daniellou, Richard</creatorcontrib><creatorcontrib>Nugier-Chauvin, Caroline</creatorcontrib><creatorcontrib>Ferrières, Vincent</creatorcontrib><creatorcontrib>Vincent, Stéphane P.</creatorcontrib><collection>Pascal-Francis</collection><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eppe, Guillaume</au><au>Peltier, Pauline</au><au>Daniellou, Richard</au><au>Nugier-Chauvin, Caroline</au><au>Ferrières, Vincent</au><au>Vincent, Stéphane P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2009-02-01</date><risdate>2009</risdate><volume>19</volume><issue>3</issue><spage>814</spage><epage>816</epage><pages>814-816</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>UDP-galactopyranose mutase (UGM) catalyzes the isomerization of UDP-galactopyranose (UDP-Gal
p) into UDP-galactofuranose (UDP-Gal
f), an essential step of the mycobacterial cell wall biosynthesis. UDP-(6-deoxy-6-fluoro)-
d-galactofuranose
1 was tested as substrate of UGM. Turnover could be observed by HPLC. The
k
cat (7.4
s
−1) and the
K
m (24
mM) of
1 were thus measured and compared with those of UDP-Gal
f and other fluorinated analogs. The presence of the fluorine atom at the 6-position had a moderate effect on the rate of the reaction but a huge one on the interactions between the enzyme and its substrate. This result demonstrated that key interactions occur at the vicinity of the 6-position of UDP-galactose in the Michaelis complex.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>19119008</pmid><doi>10.1016/j.bmcl.2008.12.014</doi><tpages>3</tpages><orcidid>https://orcid.org/0000-0002-2780-7774</orcidid><orcidid>https://orcid.org/0000-0001-7296-3736</orcidid></addata></record> |
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| ispartof | Bioorganic & medicinal chemistry letters, 2009-02, Vol.19 (3), p.814-816 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Analytical, structural and metabolic biochemistry Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Biological and medical sciences Carbohydrate Carbohydrates - chemistry Catalysis Cell Wall - metabolism Chemical Sciences Chemistry, Pharmaceutical - methods Chromatography, High Pressure Liquid Conformation Drug Design Enzymes Enzymes and enzyme inhibitors Fluorine Fluorine - chemistry Fundamental and applied biological sciences. Psychology Furans - chemistry Galactofuranose Galactose - analogs & derivatives Galactose - chemistry Intramolecular Transferases - chemistry Isomerases Kinetics Mechanism Medical sciences Molecular Conformation Mycobacterium Mycobacterium - metabolism Organic chemistry Pharmacology. Drug treatments Protein Binding Tuberculosis Uridine Diphosphate - analogs & derivatives Uridine Diphosphate - chemistry |
| title | Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose |
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