Loading…
Physiological functions of D-amino acid oxidases: from yeast to humans
D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. This enzymatic activity has been identified in most eukaryotic organisms, the only exception being plants. In the various organisms in which it does occ...
Saved in:
| Published in: | Cellular and molecular life sciences : CMLS 2007-06, Vol.64 (11), p.1373-1394 |
|---|---|
| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c515t-bc3aba409637660139f81fa86cae9d19a1426e22f4b6ce335e317f2c09bf242f3 |
|---|---|
| cites | |
| container_end_page | 1394 |
| container_issue | 11 |
| container_start_page | 1373 |
| container_title | Cellular and molecular life sciences : CMLS |
| container_volume | 64 |
| creator | Pollegioni, L Piubelli, L Sacchi, S Pilone, M. S Molla, G |
| description | D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. This enzymatic activity has been identified in most eukaryotic organisms, the only exception being plants. In the various organisms in which it does occur, DAAO fulfills distinct physiological functions: from a catabolic role in yeast cells, which allows them to grow on D-amino acids as carbon and energy sources, to a regulatory role in the human brain, where it controls the levels of the neuromodulator D-serine. Since 1935, DAAO has been the object of an astonishing number of investigations and has become a model for the dehydrogenase-oxidase class of flavoproteins. Structural and functional studies have suggested that specific physiological functions are implemented through the use of different structural elements that control access to the active site and substrate/product exchange. Current research is attempting to delineate the regulation of DAAO functions in the contest of complex biochemical and physiological networks. |
| doi_str_mv | 10.1007/s00018-007-6558-4 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11136250</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70579311</sourcerecordid><originalsourceid>FETCH-LOGICAL-c515t-bc3aba409637660139f81fa86cae9d19a1426e22f4b6ce335e317f2c09bf242f3</originalsourceid><addsrcrecordid>eNpdkUFP3DAQhS0EKrDtD-ACVg_cQj124sRcUAWlVEJqpRapN2vitXeNkhjsBLH_vl7tCgqnedJ88zQzj5AjYGfAWP0lMcagKbIsZFU1RblDDqDkrFCsht2tlg3_u08OU7rPcNVw-YHsQy2U5JwfkOtfy1XyoQsLb7CjbhrM6MOQaHD0qsDeD4Gi8XManv0ck03n1MXQ05XFNNIx0OXU45A-kj2HXbKftnVG7q6__bm8KW5_fv9x-fW2MBVUY9EagS2WTElRS8lAKNeAw0YatGoOCvPG0nLuylYaK0RlBdSOG6Zax0vuxIxcbHwfpra3c2OHMWKnH6LvMa50QK_fdga_1IvwpAFASF6x7HC6dYjhcbJp1L1PxnYdDjZMSdesqpXI9Ix8fgfehykO-TpdS2CNaITKEGwgE0NK0bqXVYDpdUZ6k5Fey3VGuswzx__f8DqxDSUDJxvAYdC4iD7pu988fyubKK4EE_8AgN2V8A</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>761083839</pqid></control><display><type>article</type><title>Physiological functions of D-amino acid oxidases: from yeast to humans</title><source>PubMed Central(OpenAccess)</source><source>Springer Link</source><creator>Pollegioni, L ; Piubelli, L ; Sacchi, S ; Pilone, M. S ; Molla, G</creator><creatorcontrib>Pollegioni, L ; Piubelli, L ; Sacchi, S ; Pilone, M. S ; Molla, G</creatorcontrib><description>D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. This enzymatic activity has been identified in most eukaryotic organisms, the only exception being plants. In the various organisms in which it does occur, DAAO fulfills distinct physiological functions: from a catabolic role in yeast cells, which allows them to grow on D-amino acids as carbon and energy sources, to a regulatory role in the human brain, where it controls the levels of the neuromodulator D-serine. Since 1935, DAAO has been the object of an astonishing number of investigations and has become a model for the dehydrogenase-oxidase class of flavoproteins. Structural and functional studies have suggested that specific physiological functions are implemented through the use of different structural elements that control access to the active site and substrate/product exchange. Current research is attempting to delineate the regulation of DAAO functions in the contest of complex biochemical and physiological networks.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-007-6558-4</identifier><identifier>PMID: 17396222</identifier><language>eng</language><publisher>Switzerland: Basel : Birkhäuser-Verlag</publisher><subject>Amino acids ; Amino Acids - chemistry ; Amino Acids - metabolism ; Animals ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Sites ; Brain - enzymology ; D-Amino acids ; D-Amino-Acid Oxidase - chemistry ; D-Amino-Acid Oxidase - classification ; D-Amino-Acid Oxidase - genetics ; D-Amino-Acid Oxidase - metabolism ; Energy sources ; Enzymatic activity ; Enzymes ; Flavin-Adenine Dinucleotide - metabolism ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Humans ; Models, Molecular ; neurotransmission ; peroxisomal enzyme ; Peroxisomes - metabolism ; Phylogeny ; physiological role ; Physiology ; Protein Conformation ; Proteins ; Review ; schizophrenia ; Substrate Specificity ; Yeasts ; Yeasts - enzymology</subject><ispartof>Cellular and molecular life sciences : CMLS, 2007-06, Vol.64 (11), p.1373-1394</ispartof><rights>Birkhäuser Verlag, Basel 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c515t-bc3aba409637660139f81fa86cae9d19a1426e22f4b6ce335e317f2c09bf242f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136250/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11136250/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17396222$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pollegioni, L</creatorcontrib><creatorcontrib>Piubelli, L</creatorcontrib><creatorcontrib>Sacchi, S</creatorcontrib><creatorcontrib>Pilone, M. S</creatorcontrib><creatorcontrib>Molla, G</creatorcontrib><title>Physiological functions of D-amino acid oxidases: from yeast to humans</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell Mol Life Sci</addtitle><description>D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. This enzymatic activity has been identified in most eukaryotic organisms, the only exception being plants. In the various organisms in which it does occur, DAAO fulfills distinct physiological functions: from a catabolic role in yeast cells, which allows them to grow on D-amino acids as carbon and energy sources, to a regulatory role in the human brain, where it controls the levels of the neuromodulator D-serine. Since 1935, DAAO has been the object of an astonishing number of investigations and has become a model for the dehydrogenase-oxidase class of flavoproteins. Structural and functional studies have suggested that specific physiological functions are implemented through the use of different structural elements that control access to the active site and substrate/product exchange. Current research is attempting to delineate the regulation of DAAO functions in the contest of complex biochemical and physiological networks.</description><subject>Amino acids</subject><subject>Amino Acids - chemistry</subject><subject>Amino Acids - metabolism</subject><subject>Animals</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Brain - enzymology</subject><subject>D-Amino acids</subject><subject>D-Amino-Acid Oxidase - chemistry</subject><subject>D-Amino-Acid Oxidase - classification</subject><subject>D-Amino-Acid Oxidase - genetics</subject><subject>D-Amino-Acid Oxidase - metabolism</subject><subject>Energy sources</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Flavin-Adenine Dinucleotide - metabolism</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>neurotransmission</subject><subject>peroxisomal enzyme</subject><subject>Peroxisomes - metabolism</subject><subject>Phylogeny</subject><subject>physiological role</subject><subject>Physiology</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Review</subject><subject>schizophrenia</subject><subject>Substrate Specificity</subject><subject>Yeasts</subject><subject>Yeasts - enzymology</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNpdkUFP3DAQhS0EKrDtD-ACVg_cQj124sRcUAWlVEJqpRapN2vitXeNkhjsBLH_vl7tCgqnedJ88zQzj5AjYGfAWP0lMcagKbIsZFU1RblDDqDkrFCsht2tlg3_u08OU7rPcNVw-YHsQy2U5JwfkOtfy1XyoQsLb7CjbhrM6MOQaHD0qsDeD4Gi8XManv0ck03n1MXQ05XFNNIx0OXU45A-kj2HXbKftnVG7q6__bm8KW5_fv9x-fW2MBVUY9EagS2WTElRS8lAKNeAw0YatGoOCvPG0nLuylYaK0RlBdSOG6Zax0vuxIxcbHwfpra3c2OHMWKnH6LvMa50QK_fdga_1IvwpAFASF6x7HC6dYjhcbJp1L1PxnYdDjZMSdesqpXI9Ix8fgfehykO-TpdS2CNaITKEGwgE0NK0bqXVYDpdUZ6k5Fey3VGuswzx__f8DqxDSUDJxvAYdC4iD7pu988fyubKK4EE_8AgN2V8A</recordid><startdate>20070601</startdate><enddate>20070601</enddate><creator>Pollegioni, L</creator><creator>Piubelli, L</creator><creator>Sacchi, S</creator><creator>Pilone, M. S</creator><creator>Molla, G</creator><general>Basel : Birkhäuser-Verlag</general><general>Springer Nature B.V</general><general>Birkhäuser-Verlag</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>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070601</creationdate><title>Physiological functions of D-amino acid oxidases: from yeast to humans</title><author>Pollegioni, L ; Piubelli, L ; Sacchi, S ; Pilone, M. S ; Molla, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c515t-bc3aba409637660139f81fa86cae9d19a1426e22f4b6ce335e317f2c09bf242f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino acids</topic><topic>Amino Acids - chemistry</topic><topic>Amino Acids - metabolism</topic><topic>Animals</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Brain - enzymology</topic><topic>D-Amino acids</topic><topic>D-Amino-Acid Oxidase - chemistry</topic><topic>D-Amino-Acid Oxidase - classification</topic><topic>D-Amino-Acid Oxidase - genetics</topic><topic>D-Amino-Acid Oxidase - metabolism</topic><topic>Energy sources</topic><topic>Enzymatic activity</topic><topic>Enzymes</topic><topic>Flavin-Adenine Dinucleotide - metabolism</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>neurotransmission</topic><topic>peroxisomal enzyme</topic><topic>Peroxisomes - metabolism</topic><topic>Phylogeny</topic><topic>physiological role</topic><topic>Physiology</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Review</topic><topic>schizophrenia</topic><topic>Substrate Specificity</topic><topic>Yeasts</topic><topic>Yeasts - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pollegioni, L</creatorcontrib><creatorcontrib>Piubelli, L</creatorcontrib><creatorcontrib>Sacchi, S</creatorcontrib><creatorcontrib>Pilone, M. S</creatorcontrib><creatorcontrib>Molla, G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular and molecular life sciences : CMLS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pollegioni, L</au><au>Piubelli, L</au><au>Sacchi, S</au><au>Pilone, M. S</au><au>Molla, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physiological functions of D-amino acid oxidases: from yeast to humans</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><addtitle>Cell Mol Life Sci</addtitle><date>2007-06-01</date><risdate>2007</risdate><volume>64</volume><issue>11</issue><spage>1373</spage><epage>1394</epage><pages>1373-1394</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>D-Amino acid oxidase (DAAO) is a FAD-containing flavoenzyme that catalyzes the oxidative deamination of D-isomers of neutral and polar amino acids. This enzymatic activity has been identified in most eukaryotic organisms, the only exception being plants. In the various organisms in which it does occur, DAAO fulfills distinct physiological functions: from a catabolic role in yeast cells, which allows them to grow on D-amino acids as carbon and energy sources, to a regulatory role in the human brain, where it controls the levels of the neuromodulator D-serine. Since 1935, DAAO has been the object of an astonishing number of investigations and has become a model for the dehydrogenase-oxidase class of flavoproteins. Structural and functional studies have suggested that specific physiological functions are implemented through the use of different structural elements that control access to the active site and substrate/product exchange. Current research is attempting to delineate the regulation of DAAO functions in the contest of complex biochemical and physiological networks.</abstract><cop>Switzerland</cop><pub>Basel : Birkhäuser-Verlag</pub><pmid>17396222</pmid><doi>10.1007/s00018-007-6558-4</doi><tpages>22</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1420-682X |
| ispartof | Cellular and molecular life sciences : CMLS, 2007-06, Vol.64 (11), p.1373-1394 |
| issn | 1420-682X 1420-9071 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11136250 |
| source | PubMed Central(OpenAccess); Springer Link |
| subjects | Amino acids Amino Acids - chemistry Amino Acids - metabolism Animals Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Brain - enzymology D-Amino acids D-Amino-Acid Oxidase - chemistry D-Amino-Acid Oxidase - classification D-Amino-Acid Oxidase - genetics D-Amino-Acid Oxidase - metabolism Energy sources Enzymatic activity Enzymes Flavin-Adenine Dinucleotide - metabolism Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Humans Models, Molecular neurotransmission peroxisomal enzyme Peroxisomes - metabolism Phylogeny physiological role Physiology Protein Conformation Proteins Review schizophrenia Substrate Specificity Yeasts Yeasts - enzymology |
| title | Physiological functions of D-amino acid oxidases: from yeast to humans |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T08%3A08%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Physiological%20functions%20of%20D-amino%20acid%20oxidases:%20from%20yeast%20to%20humans&rft.jtitle=Cellular%20and%20molecular%20life%20sciences%20:%20CMLS&rft.au=Pollegioni,%20L&rft.date=2007-06-01&rft.volume=64&rft.issue=11&rft.spage=1373&rft.epage=1394&rft.pages=1373-1394&rft.issn=1420-682X&rft.eissn=1420-9071&rft_id=info:doi/10.1007/s00018-007-6558-4&rft_dat=%3Cproquest_pubme%3E70579311%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c515t-bc3aba409637660139f81fa86cae9d19a1426e22f4b6ce335e317f2c09bf242f3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=761083839&rft_id=info:pmid/17396222&rfr_iscdi=true |