First description of betalains biosynthesis in an aquatic organism: characterization of 4,5‐DOPA‐extradiol‐dioxygenase activity in the cyanobacteria Anabaena cylindrica
This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the m...
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Published in | Microbial biotechnology Vol. 13; no. 6; pp. 1948 - 1959 |
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01.11.2020
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Abstract | This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. The discovery of this novel dioxygenase in the phylum cyanobacteria shows that betalains' formation is more diverse than expected.
Summary
The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain‐forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus. The presence of enzymes that produce these health‐promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid‐forming enzymes in organisms of different nature with no apparent relationship among them. |
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AbstractList | This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium
Anabaena cylindrica
. The enzyme showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. The discovery of this novel dioxygenase in the phylum cyanobacteria shows that betalains' formation is more diverse than expected.
The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of
Gluconacetobacter diazotrophicus
as the first betalain‐forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium
Anabaena cylindrica
. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as
G. diazotrophicus
. The presence of enzymes that produce these health‐promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid‐forming enzymes in organisms of different nature with no apparent relationship among them. The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5-DOPA-extradiol-dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain-forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L-DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus. The presence of enzymes that produce these health-promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid-forming enzymes in organisms of different nature with no apparent relationship among them. Summary The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain‐forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus. The presence of enzymes that produce these health‐promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid‐forming enzymes in organisms of different nature with no apparent relationship among them. In the present study, we expand the range of betalain‐producing bacteria describing the cloning, expression, purification, molecular and functional characterization of a DOPA‐extradiol‐dioxygenase enzyme from Anabaena cylindrica, the first cyanobacterium described producing betalamic acid. Standard dopaxanthin was followed at EIC 391.1136 m/z (C) and the same peak was detected in culture media of A. cylindrica supplemented with L‐DOPA 7.6 mM, 15 mM sodium ascorbate and 100 mM EDTA (D). [...]the existence of a betalamic acid‐forming DODA activity in A. cylindrica has been demonstrated. A. cylindrica 4,5‐DODA sequence, expression and purification The search for non‐plant L‐DOPA dioxygenases able to produce betalamic acid ‐ and thus to start the biosynthetic pathway of betalains in prokaryotes ‐ has led us to search for sequences related to that described in G. diazotrophicus. The genome of this autotrophic cyanobacterium is deposited in the NCBI database with the access number NZ_AP018166.1 (project PRJDB5665). The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5-DOPA-extradiol-dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain-forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L-DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus. The presence of enzymes that produce these health-promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid-forming enzymes in organisms of different nature with no apparent relationship among them. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. The discovery of this novel dioxygenase in the phylum cyanobacteria shows that betalains' formation is more diverse than expected. Summary The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain‐forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus. The presence of enzymes that produce these health‐promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid‐forming enzymes in organisms of different nature with no apparent relationship among them. The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These enzymes were believed to be limited to plants of the order Caryophyllales and to some fungi. However, the discovery of Gluconacetobacter diazotrophicus as the first betalain‐forming bacterium opened a new field in the search for novel biological systems able to produce betalains. This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica . The enzyme was found to be a homodimer of a polypeptide of 17.8 kDa that, opposite to previous related enzymes, showed a strong inhibition by excess of the precursor L‐DOPA. However, its heterologous expression has allowed detecting the formation of the main compounds in the biosynthetic pathway of betalains. In addition, phylogenetic analysis has shown that this enzyme is not close related to enzymes from plants, fungi or proteobacteria such as G. diazotrophicus . The presence of enzymes that produce these health‐promoting compounds is more diverse than expected. The discovery of this novel dioxygenase in the phylum cyanobacteria expands the presence of betalamic acid‐forming enzymes in organisms of different nature with no apparent relationship among them. |
Author | Gandía‐Herrero, Fernando García‐Carmona, Francisco Guerrero‐Rubio, María Alejandra |
AuthorAffiliation | 1 Departamento de Bioquímica y Biología Molecular A Unidad Docente de Biología Facultad de Veterinaria Regional Campus of International Excellence ‘Campus Mare Nostrum’ Murcia Spain |
AuthorAffiliation_xml | – name: 1 Departamento de Bioquímica y Biología Molecular A Unidad Docente de Biología Facultad de Veterinaria Regional Campus of International Excellence ‘Campus Mare Nostrum’ Murcia Spain |
Author_xml | – sequence: 1 givenname: María Alejandra surname: Guerrero‐Rubio fullname: Guerrero‐Rubio, María Alejandra organization: Regional Campus of International Excellence ‘Campus Mare Nostrum’ – sequence: 2 givenname: Francisco surname: García‐Carmona fullname: García‐Carmona, Francisco organization: Regional Campus of International Excellence ‘Campus Mare Nostrum’ – sequence: 3 givenname: Fernando orcidid: 0000-0003-4389-3454 surname: Gandía‐Herrero fullname: Gandía‐Herrero, Fernando email: fgandia@um.es organization: Regional Campus of International Excellence ‘Campus Mare Nostrum’ |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32767544$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1007/s00253-013-4961-3 10.1093/nar/gkw1132 10.1093/nar/gku340 10.1016/S0031-9422(96)00625-5 10.1093/pcp/pcp053 10.1002/cpmc.71 10.1093/nar/gkv279 10.1007/s00425-012-1593-2 10.1016/0031-9422(91)85036-Y 10.1093/nar/gku316 10.1089/jmf.2008.0280 10.1111/j.1469-8137.2011.03687.x 10.1021/jf800362t 10.1111/j.1742-4658.2005.04945.x 10.1111/nph.15159 10.1093/nar/gkl092 10.1093/nar/gkv310 10.1093/nar/gkz268 10.1016/j.tplants.2013.01.003 10.1016/0003-2697(76)90527-3 10.1104/pp.30.4.366 10.1039/C9FO02020A 10.1016/j.foodchem.2014.01.014 10.1515/znc-2007-11-1201 10.1073/pnas.1217107110 10.1016/j.foodchem.2018.09.067 10.1016/j.chroma.2005.05.013 10.1002/bies.200900167 10.1093/nar/gkz239 10.3767/003158511X578349 10.1021/np200950n 10.1016/j.phymed.2007.03.017 10.1016/0031-9422(91)84119-D 10.1007/s00425-010-1191-0 10.1111/1751-7915.13452 10.1128/mBio.00345-19 |
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Notes | Funding information This work was supported by ‘Ministerio de Ciencia e Innovación’, project AGL2017‐86526‐P (MCI/AEI/FEDER, UE) and by ‘Programa de Ayudas a Grupos de Excelencia de la Región de Murcia, Fundación Séneca, Agencia de Ciencia y Tecnología de la Región de Murcia’ (Project 19893/GERM/15). M.A.G.‐R. holds a contract financed by MEC‐FSE (Spain). ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
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References | 2010; 32 2005; 272 2010; 13 2006; 34 1997; 44 2019; 52 1991; 32 2019; 10 1991; 30 2019; 12 2017; 45 1975 2008; 56 2011; 190 2014; 154 2012; 75 2007; 14 2014; 42 2005; 1078 2013; 18 2010; 1 2009; 50 1976; 72 2015; 43 2019; 47 2010; 232 2018; 219 2011; 26 2013; 110 2007; 62 1955; 30 2012; 236 2014; 98 2019; 274 e_1_2_6_32_1 e_1_2_6_10_1 e_1_2_6_31_1 e_1_2_6_30_1 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_36_1 e_1_2_6_14_1 e_1_2_6_35_1 e_1_2_6_11_1 e_1_2_6_12_1 e_1_2_6_33_1 e_1_2_6_17_1 e_1_2_6_18_1 e_1_2_6_39_1 e_1_2_6_15_1 e_1_2_6_38_1 e_1_2_6_16_1 e_1_2_6_37_1 e_1_2_6_21_1 e_1_2_6_20_1 e_1_2_6_40_1 Segel I.H. (e_1_2_6_34_1) 1975 e_1_2_6_9_1 e_1_2_6_8_1 e_1_2_6_5_1 e_1_2_6_4_1 e_1_2_6_7_1 e_1_2_6_6_1 e_1_2_6_25_1 Miyake C. (e_1_2_6_27_1) 1991; 32 e_1_2_6_24_1 Pietrzkowski Z. (e_1_2_6_29_1) 2010; 1 e_1_2_6_3_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_22_1 e_1_2_6_28_1 e_1_2_6_26_1 |
References_xml | – volume: 18 start-page: 334 year: 2013 end-page: 343 article-title: Biosynthesis of betalains: yellow and violet plant pigments publication-title: Trends Plant Sci – volume: 13 start-page: 733 year: 2010 end-page: 739 article-title: Drinking water with red beetroot food color antagonizes esophageal carcinogenesis in N‐nitrosomethylbenzylamine‐treated rats publication-title: J Med Food – volume: 43 start-page: W580 year: 2015 end-page: W584 article-title: The EMBL‐EBI bioinformatics web and programmatic tools framework publication-title: Nucleic Acids Res – volume: 44 start-page: 567 year: 1997 end-page: 569 article-title: The formation of betalamic acid and muscaflavin by recombinant dopa‐dioxygenase from publication-title: Phytochemistry – volume: 98 start-page: 1165 year: 2014 end-page: 1174 article-title: protein YgiD produces the structural unit of plant pigments betalains: characterization of a prokaryotic enzyme with DOPA‐extradiol‐dioxygenase activity publication-title: Appl. Microbiol. Biotechnol. – volume: 272 start-page: 5101 year: 2005 end-page: 5109 article-title: Protein database searches using compositionally adjusted substitution matrices publication-title: FEBS J – volume: 32 start-page: 33 year: 1991 end-page: 43 article-title: Scavenging of hydrogen peroxide in prokaryotic and eukaryotic algae: acquisition of ascorbate peroxidase during the evolution of cyanobacteria publication-title: Plant Cell Physiol – volume: 1078 start-page: 83 year: 2005 end-page: 89 article-title: A novel method using high‐performance liquid chromatography with fluorescence detection for the determination of betaxanthins publication-title: J Chromatogr A – volume: 47 start-page: W256 year: 2019 end-page: W259 article-title: Interactive Tree Of Life (iTOL) v4: recent updates and new developments publication-title: Nucleic Acids Res – volume: 10 start-page: 8286 year: 2019 end-page: 8297 article-title: Effects of betalains on atherogenic risk factors in patients with atherosclerotic cardiovascular disease publication-title: Food Funct – volume: 42 start-page: W252 year: 2014 end-page: W258 article-title: SWISS‐MODEL: Modelling protein tertiary and quaternary structure using evolutionary information publication-title: Nucleic Acids Res – volume: 50 start-page: 1012 year: 2009 end-page: 1016 article-title: Detection of DOPA 4,5‐dioxygenase (DOD) activity using recombinant protein prepared from cells harboring cDNA encoding DOD from Mirabilis jalapa publication-title: Plant Cell Physiol – volume: 42 start-page: W320 year: 2014 end-page: W324 article-title: Deciphering key features in protein structures with the new ENDscript server publication-title: Nucleic Acids Res – volume: 32 start-page: 422 year: 2010 end-page: 429 article-title: The biological significance of substrate inhibition: a mechanism with diverse functions publication-title: BioEssays – volume: 26 start-page: 99 year: 2011 end-page: 107 article-title: Preliminary notes on dual relevance of ITS sequences and pigments in taxonomy publication-title: Persoonia – year: 1975 – volume: 154 start-page: 246 year: 2014 end-page: 254 article-title: Inactivation of lipoxygenase and cyclooxygenase by natural betalains and semi‐synthetic analogues publication-title: Food Chem – volume: 30 start-page: 366 year: 1955 end-page: 372 article-title: Studies on nitrogen‐fixing blue‐green algae. I. growth and nitrogen fixation by Lemm publication-title: Plant Physiol – volume: 110 start-page: 1053 year: 2013 end-page: 1058 article-title: Improving the coverage of the cyanobacterial phylum using diversity‐driven genome sequencing publication-title: Proc Natl Acad Sci USA – volume: 62 start-page: 779 year: 2007 end-page: 785 article-title: Pigments of fly agaric ( ) publication-title: Z Naturforsch C J Biosci – volume: 30 start-page: 1901 year: 1991 end-page: 1903 article-title: Characterization of some natural and semi‐synthetic betaxanthins publication-title: Phytochemistry – volume: 232 start-page: 449 year: 2010 end-page: 460 article-title: Structural implications on color, fluorescence, and antiradical activity in betalains publication-title: Planta – volume: 12 start-page: 993 year: 2019 end-page: 1002 article-title: Scaled‐up biotechnological production of individual betalains in a microbial system publication-title: Microb Biotechnol – volume: 1 start-page: 12 year: 2010 end-page: 17 article-title: Influence of Betalain rich extract on reduction of discomfort associated with osteoarthritis publication-title: New Med – volume: 47 start-page: W636 year: 2019 end-page: W641 article-title: The EMBL‐EBI search and sequence analysis tools APIs in 2019 publication-title: Nucleic Acids Res – volume: 190 start-page: 854 year: 2011 end-page: 864 article-title: Complex pigment evolution in the Caryophyllales publication-title: New Phytol – volume: 14 start-page: 739 year: 2007 end-page: 746 article-title: Betanin a betacyanin pigment purified from fruits of induces apoptosis in human chronic myeloid leukemia cell line‐K562 publication-title: Phytomedicine – volume: 236 start-page: 91 year: 2012 end-page: 100 article-title: Characterization of recombinant Beta vulgaris 4,5‐DOPA‐extradiol‐dioxygenase active in the biosynthesis of betalains publication-title: Planta – volume: 34 start-page: W604 year: 2006 end-page: W608 article-title: Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D‐Coffee publication-title: Nucleic Acids Res – volume: 30 start-page: 169 year: 1991 end-page: 174 article-title: Biogenesis of betalains: Purification and partial characterization of dopa 4,5‐dioxygenase from publication-title: Phytochemistry – volume: 52 year: 2019 article-title: Anabaena sp. strain PCC 7120: laboratory maintenance, cultivation, and heterocyst induction publication-title: Curr Protoc Microbiol – volume: 43 start-page: W3 year: 2015 end-page: W6 article-title: TCS: A web server for multiple sequence alignment evaluation and phylogenetic reconstruction publication-title: Nucleic Acids Res – volume: 10 year: 2019 article-title: First betalain‐producing bacteria break the exclusive presence of the pigments in the plant kingdom publication-title: MBio – volume: 274 start-page: 840 year: 2019 end-page: 847 article-title: Extension of life‐span using a RNAi model and antioxidant effect of fruit extracts and pure betalains in publication-title: Food Chem – volume: 45 start-page: D313 year: 2017 end-page: D319 article-title: The SWISS‐MODEL Repository‐new features and functionality publication-title: Nucleic Acids Res – volume: 219 start-page: 287 year: 2018 end-page: 296 article-title: Gain‐of‐function mutations in beet DODA2 identify key residues for betalain pigment evolution publication-title: New Phytol – volume: 72 start-page: 248 year: 1976 end-page: 254 article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein‐dye binding publication-title: Anal Biochem – volume: 56 start-page: 5758 year: 2008 end-page: 5764 article-title: Identification and quantification of betalains from the fruits of 10 Mexican prickly pear cultivars by high‐performance liquid chromatography and electrospray ionization mass spectrometry publication-title: J Agric Food Chem – volume: 75 start-page: 1030 year: 2012 end-page: 1036 article-title: Purification and antiradical properties of the structural unit of betalains publication-title: J Nat Prod – ident: e_1_2_6_16_1 doi: 10.1007/s00253-013-4961-3 – ident: e_1_2_6_8_1 doi: 10.1093/nar/gkw1132 – ident: e_1_2_6_7_1 doi: 10.1093/nar/gku340 – ident: e_1_2_6_28_1 doi: 10.1016/S0031-9422(96)00625-5 – ident: e_1_2_6_33_1 doi: 10.1093/pcp/pcp053 – ident: e_1_2_6_40_1 doi: 10.1002/cpmc.71 – volume-title: Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady State Enzyme Systems year: 1975 ident: e_1_2_6_34_1 contributor: fullname: Segel I.H. – ident: e_1_2_6_25_1 doi: 10.1093/nar/gkv279 – volume: 32 start-page: 33 year: 1991 ident: e_1_2_6_27_1 article-title: Scavenging of hydrogen peroxide in prokaryotic and eukaryotic algae: acquisition of ascorbate peroxidase during the evolution of cyanobacteria publication-title: Plant Cell Physiol contributor: fullname: Miyake C. – ident: e_1_2_6_14_1 doi: 10.1007/s00425-012-1593-2 – ident: e_1_2_6_38_1 doi: 10.1016/0031-9422(91)85036-Y – ident: e_1_2_6_32_1 doi: 10.1093/nar/gku316 – ident: e_1_2_6_23_1 doi: 10.1089/jmf.2008.0280 – ident: e_1_2_6_10_1 doi: 10.1111/j.1469-8137.2011.03687.x – ident: e_1_2_6_11_1 doi: 10.1021/jf800362t – ident: e_1_2_6_3_1 doi: 10.1111/j.1742-4658.2005.04945.x – ident: e_1_2_6_6_1 doi: 10.1111/nph.15159 – ident: e_1_2_6_4_1 doi: 10.1093/nar/gkl092 – ident: e_1_2_6_12_1 doi: 10.1093/nar/gkv310 – ident: e_1_2_6_26_1 doi: 10.1093/nar/gkz268 – ident: e_1_2_6_15_1 doi: 10.1016/j.tplants.2013.01.003 – ident: e_1_2_6_9_1 doi: 10.1016/0003-2697(76)90527-3 – ident: e_1_2_6_2_1 doi: 10.1104/pp.30.4.366 – ident: e_1_2_6_30_1 doi: 10.1039/C9FO02020A – ident: e_1_2_6_39_1 doi: 10.1016/j.foodchem.2014.01.014 – ident: e_1_2_6_37_1 doi: 10.1515/znc-2007-11-1201 – ident: e_1_2_6_35_1 doi: 10.1073/pnas.1217107110 – ident: e_1_2_6_21_1 doi: 10.1016/j.foodchem.2018.09.067 – ident: e_1_2_6_17_1 doi: 10.1016/j.chroma.2005.05.013 – ident: e_1_2_6_31_1 doi: 10.1002/bies.200900167 – ident: e_1_2_6_24_1 doi: 10.1093/nar/gkz239 – volume: 1 start-page: 12 year: 2010 ident: e_1_2_6_29_1 article-title: Influence of Betalain rich extract on reduction of discomfort associated with osteoarthritis publication-title: New Med contributor: fullname: Pietrzkowski Z. – ident: e_1_2_6_5_1 doi: 10.3767/003158511X578349 – ident: e_1_2_6_19_1 doi: 10.1021/np200950n – ident: e_1_2_6_36_1 doi: 10.1016/j.phymed.2007.03.017 – ident: e_1_2_6_20_1 doi: 10.1016/0031-9422(91)84119-D – ident: e_1_2_6_18_1 doi: 10.1007/s00425-010-1191-0 – ident: e_1_2_6_22_1 doi: 10.1111/1751-7915.13452 – ident: e_1_2_6_13_1 doi: 10.1128/mBio.00345-19 |
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Snippet | This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica. The enzyme... The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5-DOPA-extradiol-dioxygenase activity. These... The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity. These... In the present study, we expand the range of betalain‐producing bacteria describing the cloning, expression, purification, molecular and functional... This paper describes molecular and functional characterization of a novel dioxygenase enzyme from the aquatic cyanobacterium Anabaena cylindrica . The enzyme... Summary The biosynthesis of betalamic acid, the structural unit of pigments betalains, is performed by enzymes with 4,5‐DOPA‐extradiol‐dioxygenase activity.... |
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SubjectTerms | Anabaena Anabaena cylindrica Aquatic Organisms Ascorbic acid Betalains Biosynthesis Culture media Cyanobacteria Dihydroxyphenylalanine Dioxygenase Dioxygenases - genetics Enzymes Ethylenediaminetetraacetic acids Fungi Genomes Gluconacetobacter Levodopa Microorganisms Nitrogen Phylogenetics Phylogeny Pigments Prokaryotes Searching Sodium |
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Title | First description of betalains biosynthesis in an aquatic organism: characterization of 4,5‐DOPA‐extradiol‐dioxygenase activity in the cyanobacteria Anabaena cylindrica |
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