ins and outs of biological zinc sites
The inner shell coordination properties of zinc proteins have led to the identification of four types of zinc binding sites: catalytic, cocatalytic, structural, and protein interface. Outer shell coordination can influence the stability of the zinc site and its function as exemplified herein by the...
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| Veröffentlicht in: | Biometals 2009-02, Vol.22 (1), p.141-148 |
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| description | The inner shell coordination properties of zinc proteins have led to the identification of four types of zinc binding sites: catalytic, cocatalytic, structural, and protein interface. Outer shell coordination can influence the stability of the zinc site and its function as exemplified herein by the zinc sites in carbonic anhydrase, promatrix metalloproteases and alcohol dehydrogenase. Agents that disrupt these interactions, can lead to increased off rate constants for zinc. d-penicillamine is the first drug to inhibit a zinc protease by catalyzing the removal of the metal. Since it can accept the released zinc we have referred to it as a catalytic chelator. Agents that catalyze the release of the metal in the presence of a scavenger chelator will also inhibit enzyme catalysis and are referred to as enhanced dechelation inhibitors. |
| doi_str_mv | 10.1007/s10534-008-9184-1 |
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Agents that catalyze the release of the metal in the presence of a scavenger chelator will also inhibit enzyme catalysis and are referred to as enhanced dechelation inhibitors.</description><subject>Alcohol Dehydrogenase - chemistry</subject><subject>Alcohol Dehydrogenase - genetics</subject><subject>Alcohol Dehydrogenase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Carbonic Anhydrases - chemistry</subject><subject>Carbonic Anhydrases - genetics</subject><subject>Carbonic Anhydrases - metabolism</subject><subject>Catalysis</subject><subject>Catalysts</subject><subject>Cell Biology</subject><subject>Enzymes</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Medicine/Public Health</subject><subject>Metalloproteins - chemistry</subject><subject>Metalloproteins - metabolism</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Pharmacology/Toxicology</subject><subject>Plant Physiology</subject><subject>Protein Conformation</subject><subject>Protein Precursors - chemistry</subject><subject>Protein Precursors - genetics</subject><subject>Protein Precursors - metabolism</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Zinc</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>0966-0844</issn><issn>1572-8773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkDtPwzAUhS0EoqXwA1ggDLAZrh9x7BFVvKRKDNDZchK7cpXGJU4G-PW4SiUkBpjucL9z7rkHoXMCtwSguIsEcsYxgMSKSI7JAZqSvKBYFgU7RFNQQmCQnE_QSYxrAFAFiGM0IYpwAJJP0bVvY2baOgtDH7PgstKHJqx8ZZrsy7dVFn1v4yk6cqaJ9mw_Z2j5-PA-f8aL16eX-f0CV5yyHhtap1yUiNql4QxUYJRzJS2hcMqBync7aTmVlhlRytwwRxSUVrBKCMZm6Gb03XbhY7Cx1xsfK9s0prVhiFoIKRRw8S_IBBMpQp7Aq1_gOgxdm57QUtGUlRaJISNTdSHGzjq97fzGdJ-agN4VrceidSpa74rWJGku9r5DubH1j2LfbALoCMS0ale2-zn8l-vlKHImaLPqfNTLNwqEJUcFMtl-A5o2jpo</recordid><startdate>20090201</startdate><enddate>20090201</enddate><creator>Auld, David S</creator><general>Dordrecht : Springer Netherlands</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7U5</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20090201</creationdate><title>ins and outs of biological zinc sites</title><author>Auld, David S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-a2d100216df002fa0c0a9ffb2b07f9f095216d8e428e3a6b85a3f190be63c6633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Alcohol Dehydrogenase - chemistry</topic><topic>Alcohol Dehydrogenase - genetics</topic><topic>Alcohol Dehydrogenase - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Carbonic Anhydrases - chemistry</topic><topic>Carbonic Anhydrases - genetics</topic><topic>Carbonic Anhydrases - metabolism</topic><topic>Catalysis</topic><topic>Catalysts</topic><topic>Cell Biology</topic><topic>Enzymes</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Medicine/Public Health</topic><topic>Metalloproteins - chemistry</topic><topic>Metalloproteins - metabolism</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Pharmacology/Toxicology</topic><topic>Plant Physiology</topic><topic>Protein Conformation</topic><topic>Protein Precursors - chemistry</topic><topic>Protein Precursors - genetics</topic><topic>Protein Precursors - metabolism</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Zinc</topic><topic>Zinc - 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Academic</collection><jtitle>Biometals</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Auld, David S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ins and outs of biological zinc sites</atitle><jtitle>Biometals</jtitle><stitle>Biometals</stitle><addtitle>Biometals</addtitle><date>2009-02-01</date><risdate>2009</risdate><volume>22</volume><issue>1</issue><spage>141</spage><epage>148</epage><pages>141-148</pages><issn>0966-0844</issn><eissn>1572-8773</eissn><abstract>The inner shell coordination properties of zinc proteins have led to the identification of four types of zinc binding sites: catalytic, cocatalytic, structural, and protein interface. Outer shell coordination can influence the stability of the zinc site and its function as exemplified herein by the zinc sites in carbonic anhydrase, promatrix metalloproteases and alcohol dehydrogenase. Agents that disrupt these interactions, can lead to increased off rate constants for zinc. d-penicillamine is the first drug to inhibit a zinc protease by catalyzing the removal of the metal. Since it can accept the released zinc we have referred to it as a catalytic chelator. Agents that catalyze the release of the metal in the presence of a scavenger chelator will also inhibit enzyme catalysis and are referred to as enhanced dechelation inhibitors.</abstract><cop>Dordrecht</cop><pub>Dordrecht : Springer Netherlands</pub><pmid>19140015</pmid><doi>10.1007/s10534-008-9184-1</doi><tpages>8</tpages></addata></record> |
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| subjects | Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism Amino Acid Sequence Binding Sites Biochemistry Biomedical and Life Sciences Biophysics Carbonic Anhydrases - chemistry Carbonic Anhydrases - genetics Carbonic Anhydrases - metabolism Catalysis Catalysts Cell Biology Enzymes Humans Life Sciences Medicine/Public Health Metalloproteins - chemistry Metalloproteins - metabolism Microbiology Models, Molecular Molecular Sequence Data Pharmacology/Toxicology Plant Physiology Protein Conformation Protein Precursors - chemistry Protein Precursors - genetics Protein Precursors - metabolism Proteins Sequence Alignment Zinc Zinc - chemistry Zinc - metabolism |
| title | ins and outs of biological zinc sites |
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