In Silico＂ Characterization of 3-Phytase A and 3-Phytase B from Aspergillus niger
Phytases are used for feeding monogastric animals, because they hydrolyze phytic acid generating inorganic phosphate. Aspergillus niger 3-phytase A (PDB: 3K4Q) and 3-phytase B (PDB: 1QFX) were characterized using bioinformatic tools. Results showed that both enzymes have highly conserved catalytic p...
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| Veröffentlicht in: | Enzyme Research 2017, Vol.2017, p.1-23-007 |
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| creator | Doris C. Niño-Gómez Claudia M. Rivera-Hoyos Edwin D. Morales-Álvarez Edgar A. Reyes-Montaño Nury E. Vargas-Alejo Ingrid N. Ramírez-Casallas Kübra Erkan Türkmen Homero Sáenz-Suárez José A. Sáenz-Moreno Raúl A. Poutou-Piñales Janneth González-Santos Azucena Arévalo-Galvis |
| description | Phytases are used for feeding monogastric animals, because they hydrolyze phytic acid generating inorganic phosphate. Aspergillus niger 3-phytase A (PDB: 3K4Q) and 3-phytase B (PDB: 1QFX) were characterized using bioinformatic tools. Results showed that both enzymes have highly conserved catalytic pockets, supporting their classification as histidine acid phosphatases. 2D structures consist of 43% alpha-helix, 12% beta-sheet, and 45% others and 38% alpha-helix, 12% beta-sheet, and 50% others, respectively, and pI 4.94 and 4.60, aliphatic index 72.25 and 70.26 and average hydrophobicity of −0,304 and −0.330, respectively, suggesting aqueous media interaction. Glycosylation and glycation sites allowed detecting zones that can affect folding and biological activity, suggesting fragmentation. Docking showed that H59 and H63 act as nucleophiles and that D339 and D319 are proton donor residues. MW of 3K4Q (48.84 kDa) and 1QFX (50.78 kDa) is similar; 1QFX forms homodimers which will originate homotetramers with several catalytic center accessible to the ligand. 3K4Q is less stable (instability index 45.41) than 1QFX (instability index 33.66), but the estimated lifespan for 3K4Q is superior. Van der Waals interactions generate hydrogen bonds between the active center and O2 or H of the phytic acid phosphate groups, providing greater stability to these temporal molecular interactions. |
| doi_str_mv | 10.1155/2017/9746191 |
| format | Article |
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Niño-Gómez ; Claudia M. Rivera-Hoyos ; Edwin D. Morales-Álvarez ; Edgar A. Reyes-Montaño ; Nury E. Vargas-Alejo ; Ingrid N. Ramírez-Casallas ; Kübra Erkan Türkmen ; Homero Sáenz-Suárez ; José A. Sáenz-Moreno ; Raúl A. Poutou-Piñales ; Janneth González-Santos ; Azucena Arévalo-Galvis</creator><contributor>Chan, Sunney I.</contributor><creatorcontrib>Doris C. Niño-Gómez ; Claudia M. Rivera-Hoyos ; Edwin D. Morales-Álvarez ; Edgar A. Reyes-Montaño ; Nury E. Vargas-Alejo ; Ingrid N. Ramírez-Casallas ; Kübra Erkan Türkmen ; Homero Sáenz-Suárez ; José A. Sáenz-Moreno ; Raúl A. Poutou-Piñales ; Janneth González-Santos ; Azucena Arévalo-Galvis ; Chan, Sunney I.</creatorcontrib><description>Phytases are used for feeding monogastric animals, because they hydrolyze phytic acid generating inorganic phosphate. Aspergillus niger 3-phytase A (PDB: 3K4Q) and 3-phytase B (PDB: 1QFX) were characterized using bioinformatic tools. Results showed that both enzymes have highly conserved catalytic pockets, supporting their classification as histidine acid phosphatases. 2D structures consist of 43% alpha-helix, 12% beta-sheet, and 45% others and 38% alpha-helix, 12% beta-sheet, and 50% others, respectively, and pI 4.94 and 4.60, aliphatic index 72.25 and 70.26 and average hydrophobicity of −0,304 and −0.330, respectively, suggesting aqueous media interaction. Glycosylation and glycation sites allowed detecting zones that can affect folding and biological activity, suggesting fragmentation. Docking showed that H59 and H63 act as nucleophiles and that D339 and D319 are proton donor residues. MW of 3K4Q (48.84 kDa) and 1QFX (50.78 kDa) is similar; 1QFX forms homodimers which will originate homotetramers with several catalytic center accessible to the ligand. 3K4Q is less stable (instability index 45.41) than 1QFX (instability index 33.66), but the estimated lifespan for 3K4Q is superior. Van der Waals interactions generate hydrogen bonds between the active center and O2 or H of the phytic acid phosphate groups, providing greater stability to these temporal molecular interactions.</description><identifier>ISSN: 2090-0414</identifier><identifier>ISSN: 2090-0406</identifier><identifier>EISSN: 2090-0414</identifier><identifier>DOI: 10.1155/2017/9746191</identifier><identifier>PMID: 29348934</identifier><language>eng</language><publisher>United States: Hindawi Limiteds</publisher><subject>3-Phytase ; Acids ; Aliphatic compounds ; Animals ; Biological activity ; Catalysis ; Chemical bonds ; Docking ; Enzymes ; Eutrophication ; Fungi ; Glycosylation ; Histidine ; Hydrogen bonding ; Hydrogen bonds ; Hydrophobicity ; Life span ; Microorganisms ; Mineralization ; Molecular interactions ; Nucleophiles ; Phosphatases ; Phosphates ; Phosphorus ; Phytase ; Phytic acid ; Poultry ; Stability</subject><ispartof>Enzyme Research, 2017, Vol.2017, p.1-23-007</ispartof><rights>Copyright © 2017 Doris C. Niño-Gómez et al.</rights><rights>COPYRIGHT 2017 John Wiley & Sons, Inc.</rights><rights>Copyright © 2017 Doris C. Niño-Gómez et al.; This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2017 Doris C. Niño-Gómez et al. 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a462t-88c8974b84400852b45d68a4284d76ad5acaa39f0bc732fa2f09d28ff5a4f6563</citedby><cites>FETCH-LOGICAL-a462t-88c8974b84400852b45d68a4284d76ad5acaa39f0bc732fa2f09d28ff5a4f6563</cites><orcidid>0000-0003-0921-2125 ; 0000-0001-8841-2357</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5733987/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5733987/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,4010,27900,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29348934$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Chan, Sunney I.</contributor><creatorcontrib>Doris C. Niño-Gómez</creatorcontrib><creatorcontrib>Claudia M. Rivera-Hoyos</creatorcontrib><creatorcontrib>Edwin D. Morales-Álvarez</creatorcontrib><creatorcontrib>Edgar A. Reyes-Montaño</creatorcontrib><creatorcontrib>Nury E. Vargas-Alejo</creatorcontrib><creatorcontrib>Ingrid N. Ramírez-Casallas</creatorcontrib><creatorcontrib>Kübra Erkan Türkmen</creatorcontrib><creatorcontrib>Homero Sáenz-Suárez</creatorcontrib><creatorcontrib>José A. Sáenz-Moreno</creatorcontrib><creatorcontrib>Raúl A. Poutou-Piñales</creatorcontrib><creatorcontrib>Janneth González-Santos</creatorcontrib><creatorcontrib>Azucena Arévalo-Galvis</creatorcontrib><title>In Silico＂ Characterization of 3-Phytase A and 3-Phytase B from Aspergillus niger</title><title>Enzyme Research</title><addtitle>Enzyme Res</addtitle><description>Phytases are used for feeding monogastric animals, because they hydrolyze phytic acid generating inorganic phosphate. Aspergillus niger 3-phytase A (PDB: 3K4Q) and 3-phytase B (PDB: 1QFX) were characterized using bioinformatic tools. Results showed that both enzymes have highly conserved catalytic pockets, supporting their classification as histidine acid phosphatases. 2D structures consist of 43% alpha-helix, 12% beta-sheet, and 45% others and 38% alpha-helix, 12% beta-sheet, and 50% others, respectively, and pI 4.94 and 4.60, aliphatic index 72.25 and 70.26 and average hydrophobicity of −0,304 and −0.330, respectively, suggesting aqueous media interaction. Glycosylation and glycation sites allowed detecting zones that can affect folding and biological activity, suggesting fragmentation. Docking showed that H59 and H63 act as nucleophiles and that D339 and D319 are proton donor residues. MW of 3K4Q (48.84 kDa) and 1QFX (50.78 kDa) is similar; 1QFX forms homodimers which will originate homotetramers with several catalytic center accessible to the ligand. 3K4Q is less stable (instability index 45.41) than 1QFX (instability index 33.66), but the estimated lifespan for 3K4Q is superior. Van der Waals interactions generate hydrogen bonds between the active center and O2 or H of the phytic acid phosphate groups, providing greater stability to these temporal molecular interactions.</description><subject>3-Phytase</subject><subject>Acids</subject><subject>Aliphatic compounds</subject><subject>Animals</subject><subject>Biological activity</subject><subject>Catalysis</subject><subject>Chemical bonds</subject><subject>Docking</subject><subject>Enzymes</subject><subject>Eutrophication</subject><subject>Fungi</subject><subject>Glycosylation</subject><subject>Histidine</subject><subject>Hydrogen bonding</subject><subject>Hydrogen bonds</subject><subject>Hydrophobicity</subject><subject>Life span</subject><subject>Microorganisms</subject><subject>Mineralization</subject><subject>Molecular interactions</subject><subject>Nucleophiles</subject><subject>Phosphatases</subject><subject>Phosphates</subject><subject>Phosphorus</subject><subject>Phytase</subject><subject>Phytic acid</subject><subject>Poultry</subject><subject>Stability</subject><issn>2090-0414</issn><issn>2090-0406</issn><issn>2090-0414</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkltrFDEUxwdRbKl981kGfBF02lwnyYuwXbwUKhaqz-HsTLKbMpOsyYxSH_1cfie_ghl3XXdFMBeSk_zOPznJKYrHGJ1hzPk5QVicK8FqrPC94pgghSrEMLu_Nz8qTlO6RblQlVv9sDgiijKZ-3Fxc-nLG9e5Jvz4_q2cryBCM5jovsLggi-DLWl1vbobIJlyVoJv9-yL0sbQl7O0NnHpum5MpXdLEx8VDyx0yZxux5Pi4-tXH-Zvq6v3by7ns6sKWE2GSspG5qsvJGMISU4WjLe1BEYka0UNLYcGgCqLFo2gxAKxSLVEWsuB2ZrX9KR4udFdj4vetI3xQ4ROr6PrId7pAE4f7ni30svwWXNBqZIiCzzbCsTwaTRp0L1Ljek68CaMSWMlFVdEMZ7Rp3-ht2GMPoeXKUE5pjj3HbWEzmjnbcjnNpOonnFOBc9yk9bZP6hcW9Pnj_DGurx-4PBi49DEkFI0dhcjRnrKAz3lgd7mQcaf7L_LDv796xl4vgFWzrfwxf1P7t2GBhfd4P4Efp0xjgkSCOFfLphMg0SSkLyED41sUo2QoD8BB2XMrg</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Doris C. 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Niño-Gómez</au><au>Claudia M. Rivera-Hoyos</au><au>Edwin D. Morales-Álvarez</au><au>Edgar A. Reyes-Montaño</au><au>Nury E. Vargas-Alejo</au><au>Ingrid N. Ramírez-Casallas</au><au>Kübra Erkan Türkmen</au><au>Homero Sáenz-Suárez</au><au>José A. Sáenz-Moreno</au><au>Raúl A. Poutou-Piñales</au><au>Janneth González-Santos</au><au>Azucena Arévalo-Galvis</au><au>Chan, Sunney I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In Silico＂ Characterization of 3-Phytase A and 3-Phytase B from Aspergillus niger</atitle><jtitle>Enzyme Research</jtitle><addtitle>Enzyme Res</addtitle><date>2017</date><risdate>2017</risdate><volume>2017</volume><spage>1</spage><epage>23-007</epage><pages>1-23-007</pages><issn>2090-0414</issn><issn>2090-0406</issn><eissn>2090-0414</eissn><abstract>Phytases are used for feeding monogastric animals, because they hydrolyze phytic acid generating inorganic phosphate. Aspergillus niger 3-phytase A (PDB: 3K4Q) and 3-phytase B (PDB: 1QFX) were characterized using bioinformatic tools. Results showed that both enzymes have highly conserved catalytic pockets, supporting their classification as histidine acid phosphatases. 2D structures consist of 43% alpha-helix, 12% beta-sheet, and 45% others and 38% alpha-helix, 12% beta-sheet, and 50% others, respectively, and pI 4.94 and 4.60, aliphatic index 72.25 and 70.26 and average hydrophobicity of −0,304 and −0.330, respectively, suggesting aqueous media interaction. Glycosylation and glycation sites allowed detecting zones that can affect folding and biological activity, suggesting fragmentation. Docking showed that H59 and H63 act as nucleophiles and that D339 and D319 are proton donor residues. MW of 3K4Q (48.84 kDa) and 1QFX (50.78 kDa) is similar; 1QFX forms homodimers which will originate homotetramers with several catalytic center accessible to the ligand. 3K4Q is less stable (instability index 45.41) than 1QFX (instability index 33.66), but the estimated lifespan for 3K4Q is superior. Van der Waals interactions generate hydrogen bonds between the active center and O2 or H of the phytic acid phosphate groups, providing greater stability to these temporal molecular interactions.</abstract><cop>United States</cop><pub>Hindawi Limiteds</pub><pmid>29348934</pmid><doi>10.1155/2017/9746191</doi><tpages>23</tpages><orcidid>https://orcid.org/0000-0003-0921-2125</orcidid><orcidid>https://orcid.org/0000-0001-8841-2357</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Enzyme Research, 2017, Vol.2017, p.1-23-007 |
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| source | Wiley Online Library Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection; PubMed Central Open Access |
| subjects | 3-Phytase Acids Aliphatic compounds Animals Biological activity Catalysis Chemical bonds Docking Enzymes Eutrophication Fungi Glycosylation Histidine Hydrogen bonding Hydrogen bonds Hydrophobicity Life span Microorganisms Mineralization Molecular interactions Nucleophiles Phosphatases Phosphates Phosphorus Phytase Phytic acid Poultry Stability |
| title | In Silico＂ Characterization of 3-Phytase A and 3-Phytase B from Aspergillus niger |
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