Engineering an aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid
3-Hydroxypropionic acid (3-HP) can be produced via the biological route involving two enzymatic reactions: dehydration of glycerol to 3-hydroxypropanal (3-HPA) and then oxidation to 3-HP. However, commercial production of 3-HP using recombinant microorganisms has been hampered with several problems,...
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| creator | Park, Ye Seop Choi, Un Jong Nam, Nguyen Hoai Choi, Sang Jin Nasir, Abdul Lee, Sun-Gu Kim, Kyung Jin Jung, Gyoo Yeol Choi, Sangdun Shim, Jeung Yeop Park, Sunghoon Yoo, Tae Hyeon |
| description | 3-Hydroxypropionic acid (3-HP) can be produced via the biological route involving two enzymatic reactions: dehydration of glycerol to 3-hydroxypropanal (3-HPA) and then oxidation to 3-HP. However, commercial production of 3-HP using recombinant microorganisms has been hampered with several problems, some of which are associated with the toxicity of 3-HPA and the efficiency of NAD
+
regeneration. We engineered α-ketoglutaric semialdehyde dehydrogenase (KGSADH) from
Azospirillum brasilense
for the second reaction to address these issues. The residues in the binding sites for the substrates, 3-HPA and NAD
+
, were randomized, and the resulting libraries were screened for higher activity. Isolated KGSADH variants had significantly lower K
m
values for both the substrates. The enzymes also showed higher substrate specificities for aldehyde and NAD
+
, less inhibition by NADH, and greater resistance to inactivation by 3-HPA than the wild-type enzyme. A recombinant
Pseudomonas denitrificans
strain with one of the engineered KGSADH variants exhibited less accumulation of 3-HPA, decreased levels of inactivation of the enzymes, and higher cell growth than that with the wild-type KGSADH. The flask culture of the
P. denitrificans
strain with the mutant KGSADH resulted in about 40% increase of 3-HP titer (53 mM) compared with that using the wild-type enzyme (37 mM). |
| doi_str_mv | 10.1038/s41598-017-15400-x |
| format | Article |
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+
regeneration. We engineered α-ketoglutaric semialdehyde dehydrogenase (KGSADH) from
Azospirillum brasilense
for the second reaction to address these issues. The residues in the binding sites for the substrates, 3-HPA and NAD
+
, were randomized, and the resulting libraries were screened for higher activity. Isolated KGSADH variants had significantly lower K
m
values for both the substrates. The enzymes also showed higher substrate specificities for aldehyde and NAD
+
, less inhibition by NADH, and greater resistance to inactivation by 3-HPA than the wild-type enzyme. A recombinant
Pseudomonas denitrificans
strain with one of the engineered KGSADH variants exhibited less accumulation of 3-HPA, decreased levels of inactivation of the enzymes, and higher cell growth than that with the wild-type KGSADH. The flask culture of the
P. denitrificans
strain with the mutant KGSADH resulted in about 40% increase of 3-HP titer (53 mM) compared with that using the wild-type enzyme (37 mM).</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-017-15400-x</identifier><identifier>PMID: 29214999</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>3-Hydroxypropionaldehyde ; 42/70 ; 631/45/603 ; 631/61/318 ; 82/47 ; 82/80 ; 82/83 ; Aldehyde dehydrogenase ; Aldehyde Oxidoreductases - chemistry ; Aldehyde Oxidoreductases - metabolism ; Azospirillum brasilense - enzymology ; Bacterial Proteins - metabolism ; Binding sites ; Cell culture ; Dehydration ; Dehydrogenase ; Dehydrogenases ; Enzymes ; Glyceraldehyde - analogs & derivatives ; Glyceraldehyde - metabolism ; Glycerol ; Glycerol - metabolism ; Humanities and Social Sciences ; Inactivation ; Ketoglutaric acid ; Lactic Acid - analogs & derivatives ; Lactic Acid - metabolism ; Microorganisms ; multidisciplinary ; NAD ; NAD - metabolism ; NADH ; Oxidation ; Propane - metabolism ; Protein Conformation ; Protein Engineering - methods ; Science ; Science (multidisciplinary) ; Substrate Specificity ; Substrates ; Toxicity</subject><ispartof>Scientific reports, 2017-12, Vol.7 (1), p.17155-12, Article 17155</ispartof><rights>The Author(s) 2017</rights><rights>2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-82551d2f9bcf17a83d84a1d7b312d307be01144aeea1e9d9e22e585041508cea3</citedby><cites>FETCH-LOGICAL-c540t-82551d2f9bcf17a83d84a1d7b312d307be01144aeea1e9d9e22e585041508cea3</cites><orcidid>0000-0002-2339-3500</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/PMC5719400/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5719400/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29214999$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Ye Seop</creatorcontrib><creatorcontrib>Choi, Un Jong</creatorcontrib><creatorcontrib>Nam, Nguyen Hoai</creatorcontrib><creatorcontrib>Choi, Sang Jin</creatorcontrib><creatorcontrib>Nasir, Abdul</creatorcontrib><creatorcontrib>Lee, Sun-Gu</creatorcontrib><creatorcontrib>Kim, Kyung Jin</creatorcontrib><creatorcontrib>Jung, Gyoo Yeol</creatorcontrib><creatorcontrib>Choi, Sangdun</creatorcontrib><creatorcontrib>Shim, Jeung Yeop</creatorcontrib><creatorcontrib>Park, Sunghoon</creatorcontrib><creatorcontrib>Yoo, Tae Hyeon</creatorcontrib><title>Engineering an aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>3-Hydroxypropionic acid (3-HP) can be produced via the biological route involving two enzymatic reactions: dehydration of glycerol to 3-hydroxypropanal (3-HPA) and then oxidation to 3-HP. However, commercial production of 3-HP using recombinant microorganisms has been hampered with several problems, some of which are associated with the toxicity of 3-HPA and the efficiency of NAD
+
regeneration. We engineered α-ketoglutaric semialdehyde dehydrogenase (KGSADH) from
Azospirillum brasilense
for the second reaction to address these issues. The residues in the binding sites for the substrates, 3-HPA and NAD
+
, were randomized, and the resulting libraries were screened for higher activity. Isolated KGSADH variants had significantly lower K
m
values for both the substrates. The enzymes also showed higher substrate specificities for aldehyde and NAD
+
, less inhibition by NADH, and greater resistance to inactivation by 3-HPA than the wild-type enzyme. A recombinant
Pseudomonas denitrificans
strain with one of the engineered KGSADH variants exhibited less accumulation of 3-HPA, decreased levels of inactivation of the enzymes, and higher cell growth than that with the wild-type KGSADH. The flask culture of the
P. denitrificans
strain with the mutant KGSADH resulted in about 40% increase of 3-HP titer (53 mM) compared with that using the wild-type enzyme (37 mM).</description><subject>3-Hydroxypropionaldehyde</subject><subject>42/70</subject><subject>631/45/603</subject><subject>631/61/318</subject><subject>82/47</subject><subject>82/80</subject><subject>82/83</subject><subject>Aldehyde dehydrogenase</subject><subject>Aldehyde Oxidoreductases - chemistry</subject><subject>Aldehyde Oxidoreductases - metabolism</subject><subject>Azospirillum brasilense - enzymology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding sites</subject><subject>Cell culture</subject><subject>Dehydration</subject><subject>Dehydrogenase</subject><subject>Dehydrogenases</subject><subject>Enzymes</subject><subject>Glyceraldehyde - analogs & derivatives</subject><subject>Glyceraldehyde - metabolism</subject><subject>Glycerol</subject><subject>Glycerol - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Inactivation</subject><subject>Ketoglutaric acid</subject><subject>Lactic Acid - analogs & derivatives</subject><subject>Lactic Acid - metabolism</subject><subject>Microorganisms</subject><subject>multidisciplinary</subject><subject>NAD</subject><subject>NAD - metabolism</subject><subject>NADH</subject><subject>Oxidation</subject><subject>Propane - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Engineering - methods</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Substrate 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aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid</title><author>Park, Ye Seop ; Choi, Un Jong ; Nam, Nguyen Hoai ; Choi, Sang Jin ; Nasir, Abdul ; Lee, Sun-Gu ; Kim, Kyung Jin ; Jung, Gyoo Yeol ; Choi, Sangdun ; Shim, Jeung Yeop ; Park, Sunghoon ; Yoo, Tae Hyeon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c540t-82551d2f9bcf17a83d84a1d7b312d307be01144aeea1e9d9e22e585041508cea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>3-Hydroxypropionaldehyde</topic><topic>42/70</topic><topic>631/45/603</topic><topic>631/61/318</topic><topic>82/47</topic><topic>82/80</topic><topic>82/83</topic><topic>Aldehyde dehydrogenase</topic><topic>Aldehyde Oxidoreductases - chemistry</topic><topic>Aldehyde Oxidoreductases - metabolism</topic><topic>Azospirillum brasilense - enzymology</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding sites</topic><topic>Cell culture</topic><topic>Dehydration</topic><topic>Dehydrogenase</topic><topic>Dehydrogenases</topic><topic>Enzymes</topic><topic>Glyceraldehyde - analogs & derivatives</topic><topic>Glyceraldehyde - metabolism</topic><topic>Glycerol</topic><topic>Glycerol - metabolism</topic><topic>Humanities and Social Sciences</topic><topic>Inactivation</topic><topic>Ketoglutaric acid</topic><topic>Lactic Acid - analogs & derivatives</topic><topic>Lactic Acid - metabolism</topic><topic>Microorganisms</topic><topic>multidisciplinary</topic><topic>NAD</topic><topic>NAD - metabolism</topic><topic>NADH</topic><topic>Oxidation</topic><topic>Propane - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Engineering - methods</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Ye Seop</creatorcontrib><creatorcontrib>Choi, Un Jong</creatorcontrib><creatorcontrib>Nam, Nguyen Hoai</creatorcontrib><creatorcontrib>Choi, Sang Jin</creatorcontrib><creatorcontrib>Nasir, Abdul</creatorcontrib><creatorcontrib>Lee, Sun-Gu</creatorcontrib><creatorcontrib>Kim, Kyung Jin</creatorcontrib><creatorcontrib>Jung, Gyoo Yeol</creatorcontrib><creatorcontrib>Choi, Sangdun</creatorcontrib><creatorcontrib>Shim, Jeung Yeop</creatorcontrib><creatorcontrib>Park, Sunghoon</creatorcontrib><creatorcontrib>Yoo, Tae Hyeon</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE 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Rep</addtitle><date>2017-12-07</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>17155</spage><epage>12</epage><pages>17155-12</pages><artnum>17155</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>3-Hydroxypropionic acid (3-HP) can be produced via the biological route involving two enzymatic reactions: dehydration of glycerol to 3-hydroxypropanal (3-HPA) and then oxidation to 3-HP. However, commercial production of 3-HP using recombinant microorganisms has been hampered with several problems, some of which are associated with the toxicity of 3-HPA and the efficiency of NAD
+
regeneration. We engineered α-ketoglutaric semialdehyde dehydrogenase (KGSADH) from
Azospirillum brasilense
for the second reaction to address these issues. The residues in the binding sites for the substrates, 3-HPA and NAD
+
, were randomized, and the resulting libraries were screened for higher activity. Isolated KGSADH variants had significantly lower K
m
values for both the substrates. The enzymes also showed higher substrate specificities for aldehyde and NAD
+
, less inhibition by NADH, and greater resistance to inactivation by 3-HPA than the wild-type enzyme. A recombinant
Pseudomonas denitrificans
strain with one of the engineered KGSADH variants exhibited less accumulation of 3-HPA, decreased levels of inactivation of the enzymes, and higher cell growth than that with the wild-type KGSADH. The flask culture of the
P. denitrificans
strain with the mutant KGSADH resulted in about 40% increase of 3-HP titer (53 mM) compared with that using the wild-type enzyme (37 mM).</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29214999</pmid><doi>10.1038/s41598-017-15400-x</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-2339-3500</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Scientific reports, 2017-12, Vol.7 (1), p.17155-12, Article 17155 |
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| source | MEDLINE; Nature Free; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; Springer Nature OA Free Journals |
| subjects | 3-Hydroxypropionaldehyde 42/70 631/45/603 631/61/318 82/47 82/80 82/83 Aldehyde dehydrogenase Aldehyde Oxidoreductases - chemistry Aldehyde Oxidoreductases - metabolism Azospirillum brasilense - enzymology Bacterial Proteins - metabolism Binding sites Cell culture Dehydration Dehydrogenase Dehydrogenases Enzymes Glyceraldehyde - analogs & derivatives Glyceraldehyde - metabolism Glycerol Glycerol - metabolism Humanities and Social Sciences Inactivation Ketoglutaric acid Lactic Acid - analogs & derivatives Lactic Acid - metabolism Microorganisms multidisciplinary NAD NAD - metabolism NADH Oxidation Propane - metabolism Protein Conformation Protein Engineering - methods Science Science (multidisciplinary) Substrate Specificity Substrates Toxicity |
| title | Engineering an aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid |
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