Putrescine Transaminases for the Synthesis of Saturated Nitrogen Heterocycles from Polyamines

Putrescine transaminase (pATA; EC 2.6.1.82) catalyzes the transfer of an amino group from terminal diamine donor molecules to keto acid acceptors by using pyridoxal‐5′‐phosphate as a cofactor. The ygjG genes from Escherichia coli K12, Bacillus megaterium, and Bacillus mycoides were successfully cloned and expressed in E. coli BL21(DE3) cells. The three putrescine transaminases were all shown to prefer diaminoalkanes as substrates and thereby generated cyclic imines from the ω‐amino aldehyde intermediates. The addition of a mild chemical reducing agent rapidly reduced the imine intermediate in situ to furnish a range of N‐heterocycle products. We applied pATA in a biomimetic synthesis of 2,3‐dihydro‐1H‐indolizinium‐containing targets, notably the bioactive alkaloid ficuseptine.

[1]  W. Kroutil,et al.  The Industrial Age of Biocatalytic Transamination , 2015, European journal of organic chemistry.

[2]  U. Bornscheuer,et al.  Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications. , 2015, Biotechnology advances.

[3]  A. Peracchi,et al.  A subfamily of PLP-dependent enzymes specialized in handling terminal amines. , 2015, Biochimica et biophysica acta.

[4]  E. Gravel,et al.  Manipulating Simple Reactive Chemical Units: Fishing for Alkaloids from Complex Mixtures. , 2015, Chemistry.

[5]  Wolfgang Kroutil,et al.  Biocatalytic Imine Reduction and Reductive Amination of Ketones , 2015 .

[6]  N. Turner,et al.  An (R)‐Imine Reductase Biocatalyst for the Asymmetric Reduction of Cyclic Imines , 2015, ChemCatChem.

[7]  H. J. Cha,et al.  Structure of Putrescine Aminotransferase from Escherichia coli Provides Insights into the Substrate Specificity among Class III Aminotransferases , 2014, PloS one.

[8]  D. Gamenara,et al.  Enantioselective imine reduction catalyzed by imine reductases and artificial metalloenzymes. , 2014, Organic & biomolecular chemistry.

[9]  Andy Wells,et al.  The Enzyme Spring: Biocatalysis at its Best , 2014 .

[10]  N. Turner,et al.  Development of an R‐Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity , 2014 .

[11]  H. Kohls,et al.  Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis. , 2014, Current opinion in chemical biology.

[12]  J. Bode,et al.  Synthesis of saturated N-heterocycles. , 2014, The Journal of organic chemistry.

[13]  Nicholas J. Turner,et al.  Biocatalytic Approaches to the Synthesis of Enantiomerically Pure Chiral Amines , 2014, Topics in Catalysis.

[14]  Nicholas J Turner,et al.  A Regio- and Stereoselective ω-Transaminase/Monoamine Oxidase Cascade for the Synthesis of Chiral 2,5-Disubstituted Pyrrolidines , 2014, Angewandte Chemie.

[15]  Wolfgang Kroutil,et al.  Recent Developments of Cascade Reactions Involving ω‑Transaminases , 2014 .

[16]  N. Turner,et al.  Asymmetric Reduction of Cyclic Imines Catalyzed by a Whole‐Cell Biocatalyst Containing an (S)‐Imine Reductase , 2013 .

[17]  Nicholas J. Turner,et al.  Engineering an enantioselective amine oxidase for the synthesis of pharmaceutical building blocks and alkaloid natural products. , 2013, Journal of the American Chemical Society.

[18]  Hiroaki Yamamoto,et al.  A NADPH-dependent (S)-imine reductase (SIR) from Streptomyces sp. GF3546 for asymmetric synthesis of optically active amines: purification, characterization, gene cloning, and expression , 2012, Applied Microbiology and Biotechnology.

[19]  T. Nagasawa,et al.  Purification and Characterization of a Novel (R)-Imine Reductase from Streptomyces sp. GF3587 , 2011, Bioscience, biotechnology, and biochemistry.

[20]  Volker F. Wendisch,et al.  Biotechnological production of polyamines by Bacteria: recent achievements and future perspectives , 2011, Applied Microbiology and Biotechnology.

[21]  Stephen D Pickett,et al.  The impact of aromatic ring count on compound developability: further insights by examining carbo- and hetero-aromatic and -aliphatic ring types. , 2011, Drug discovery today.

[22]  M. Truppo,et al.  A fast and sensitive assay for measuring the activity and enantioselectivity of transaminases. , 2011, Chemical communications.

[23]  S. Lee,et al.  Metabolic engineering of Escherichia coli for the production of putrescine: a four carbon diamine. , 2009, Biotechnology and bioengineering.

[24]  Wolfgang Kroutil,et al.  Asymmetric Synthesis of Optically Pure Pharmacologically Relevant Amines Employing ω‐Transaminases , 2008 .

[25]  Ramesh N. Patel,et al.  Preparation of (R)-Amines from Racemic Amines with an (S)-Amine Transaminase from Bacillus megaterium , 2008 .

[26]  Mark E. B. Smith,et al.  Substrate spectrum of ω-transaminase from Chromobacterium violaceum DSM30191 and its potential for biocatalysis , 2007 .

[27]  S. Smirnov,et al.  Identification of Escherichia coli K12 YdcW protein as a γ‐aminobutyraldehyde dehydrogenase , 2005 .

[28]  B. Snider,et al.  Syntheses of ficuseptine, juliprosine, and juliprosopine by biomimetic intramolecular Chichibabin pyridine syntheses. , 2005, Organic letters.

[29]  Seongyop Lim,et al.  ω-Amino Acid:Pyruvate Transaminase from Alcaligenes denitrificans Y2k-2: a New Catalyst for Kinetic Resolution of β-Amino Acids and Amines , 2004, Applied and Environmental Microbiology.

[30]  B. Berger,et al.  Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis , 2003, BMC Microbiology.

[31]  F. Bracher,et al.  Total Synthesis of the Indolizidinium Alkaloid Ficuseptine , 2002 .

[32]  T. Leisinger,et al.  Role of 4-aminobutyrate aminotransferase in the arginine metabolism of Pseudomonas aeruginosa , 1976, Journal of bacteriology.

[33]  M. O'Leary.  A proposed structure for the 330 -nm chromophore of glutamate decarboxylase and other pyridoxal 5'-phosphate dependent enzymes. , 1971, Biochimica et biophysica acta.

[34]  K. Kim,et al.  PURIFICATION AND PROPERTIES OF A DIAMINE ALPHA-KETOGLUTARATE TRANSAMINASE FROM ESCHERICHIA COLI. , 1964, The Journal of biological chemistry.

[35]  C. Schöpf,et al.  Der Übergang von Δ1‐Piperidein in Tetrahydro‐anabasin unter zellmöglichen Bedingungen , 1956 .

[36]  S. Godtfredsen,et al.  Ullmann ' s Encyclopedia of Industrial Chemistry , 2017 .