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Cited by 25Origins and Evolution of LifeRNA and protein synthesis mechanismsChemical Reaction Mechanisms

Prebiotic Synthesis of Aspartate Using Life’s Metabolism as a Guide

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Harrison, Stuart A., Webb, William L., Rammu, Hanadi, Lane, Nick·2023·Life
DOI 10.3390/life13051177PMC PMC10221237
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Abstract

A protometabolic approach to the origins of life assumes that the conserved biochemistry of metabolism has direct continuity with prebiotic chemistry. One of the most important amino acids in modern biology is aspartic acid, serving as a nodal metabolite for the synthesis of many other essential biomolecules. Aspartate’s prebiotic synthesis is complicated by the instability of its precursor, oxaloacetate. In this paper, we show that the use of the biologically relevant cofactor pyridoxamine, supported by metal ion catalysis, is sufficiently fast to offset oxaloacetate’s degradation. Cu2+-catalysed transamination of oxaloacetate by pyridoxamine achieves around a 5% yield within 1 h, and can operate across a broad range of pH, temperature, and pressure. In addition, the synthesis of the downstream product β-alanine may also take place in the same reaction system at very low yields, directly mimicking an archaeal synthesis route. Amino group transfer supported by pyridoxal is shown to take place from aspartate to alanine, but the reverse reaction (alanine to aspartate) shows a poor yield. Overall, our results show that the nodal metabolite aspartate and related amino acids can indeed be synthesised via protometabolic pathways that foreshadow modern metabolism in the presence of the simple cofactor pyridoxamine and metal ions.

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  • Nucleic acid synthesis that might underpin an RNA world is more challenging under hydrothermal vent conditions.

    “Nucleic acid synthesis that might underpin an RNA world is more challenging under hydrothermal vent conditions (Muchowska et al., 2020; Yi et al., 2022; Harrison et al., 2023) but at the same time, there is no clear evidence that an RNA world ever existed (Baross and Martin, 2015) and there are no self-replicating RNA molecules in any life form as far as we know.”

    From Serpentinization as the source of energy, electrons, organics, catalysts, nutrients and pH gradients for the origin of LUCA and life (2023) · cites this paper as Harrison et al., 2023

    The Introduction (§1.1) discusses the goal of synthesizing nucleotides through protometabolic chemistry, and the Discussion (§4.2) considers hydrothermal conditions for aspartate synthesis. Neither addresses whether nucleic acid synthesis for a possible RNA world is more challenging at hydrothermal vents. Searches for RNA-world and nucleic-acid synthesis under hydrothermal conditions found no passage making that comparison. (LLM, conf=0.74)

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  1. [3]Harrison S.A. Palmeira R.N. Halpern A. Lane N. A biophysical basis for the emergence of the genetic code in protocells Biochim. Biophys. Acta Bioenerg. 2022 1863 148597 10.1016/j.bbabio.2022.148597 35868450 · DOI
  2. [4]Belousoff M. Davidovich C. Zimmerman E. Caspi Y. Wekselman I. Rozenszajn L. Shapira T. Sade-Falk O. Taha L. Bashan A. Ancient machinery embedded in the contemporary ribosome Biochem. Soc. Trans. 2010 38 422 427 10.1042/BST0380422 20298195 · DOI
  3. [5]Bose T. Fridkin G. Davidovich C. Krupkin M. Dinger N. Falkovich A.H. Peleg Y. Agmon I. Bashan A. Yonath A. Origin of life: Protoribosome forms peptide bonds and links RNA and protein dominated worlds Nucleic Acids Res. 2022 50 1815 1828 10.1093/nar/gkac052 35137169 PMC8886871 · DOI
  4. [6]Anantharaman V. Koonin E.V. Aravind L. Comparative genomics and evolution of proteins involved in RNA metabolism Nucleic Acids Res. 2002 30 1427 1464 10.1093/nar/30.7.1427 11917006 PMC101826 · DOI · Paper page
  5. [7]Koonin E.V. Krupovic M. Ishino S. Ishino Y. The replication machinery of LUCA: Common origin of DNA replication and transcription BMC Biol. 2020 18 61 10.1186/s12915-020-00800-9 32517760 PMC7281927 · DOI
  6. [8]Wimmer J.L.E. Vieira A.D.N. Xavier J.C. Kleinermanns K. Martin W.F. Preiner M. The Autotrophic Core: An Ancient Network of 404 Reactions Converts H2, CO2, and NH3 into Amino Acids, Bases, and Cofactors Microorganisms 2021 9 458 10.3390/microorganisms9020458 33672143 PMC7926472 · DOI · Paper page
  7. [9]Braakman R. Smith E. The compositional and evolutionary logic of metabolism Phys. Biol. 2012 10 011001 10.1088/1478-3975/10/1/011001 23234798 · DOI · Paper page
  8. [10]Braakman R. Smith E. The Emergence and Early Evolution of Biological Carbon-Fixation PLoS Comput. Biol. 2012 8 e1002455 10.1371/journal.pcbi.1002455 22536150 PMC3334880 · DOI · Paper page
  9. [16]Xavier J.C. Hordijk W. Kauffman S. Steel M. Martin W.F. Autocatalytic chemical networks at the origin of metabolism Proc. R. Soc. B Boil. Sci. 2020 287 20192377 10.1098/rspb.2019.2377 PMC7126077 32156207 · DOI · Paper page
  10. [18]Muchowska K.B. Varma S.J. Chevallot-Beroux E. Lethuillier-Karl L. Li G. Moran J. Metals promote sequences of the reverse Krebs cycle Nat. Ecol. Evol. 2017 1 1716 1721 10.1038/s41559-017-0311-7 28970480 PMC5659384 · DOI · Paper page
  11. [19]Keller M.A. Kampjut D. Harrison S.A. Ralser M. Sulfate radicals enable a non-enzymatic Krebs cycle precursor Nat. Ecol. Evol. 2017 1 83 10.1038/s41559-017-0083 28584880 PMC5455955 · DOI
  12. [20]Muchowska K.B. Varma S.J. Moran J. Synthesis and breakdown of universal metabolic precursors promoted by iron Nature 2019 569 104 107 10.1038/s41586-019-1151-1 31043728 PMC6517266 · DOI · Paper page
  13. [21]Mayer R.J. Kaur H. Rauscher S.A. Moran J. Mechanistic Insight into Metal Ion-Catalyzed Transamination J. Am. Chem. Soc. 2021 143 19099 19111 10.1021/jacs.1c08535 34730975 · DOI · Paper page
  14. [22]Yi J. Kaur H. Kazöne W. Rauscher S.A. Gravillier L. Muchowska K.B. Moran J. A Nonenzymatic Analog of Pyrimidine Nucleobase Biosynthesis Angew. Chem. Int. Ed. 2022 61 e202117211 10.1002/anie.202117211 PMC9325535 35304939 · DOI
  15. [23]Whicher A. Camprubi E. Pinna S. Herschy B. Lane N. Acetyl Phosphate as a Primordial Energy Currency at the Origin of Life Orig. Life Evol. Biosph. 2018 48 159 179 10.1007/s11084-018-9555-8 29502283 PMC6061221 · DOI · Paper page
  16. [28]Rauscher S.A. Moran J. Hydrogen Drives Part of the Reverse Krebs Cycle under Metal or Meteorite Catalysis Angew. Chem. Int. Ed. 2022 61 e202212932 10.1002/anie.202212932 PMC10100321 36251920 · DOI · Paper page
  17. [30]West T.O. Sojo V. Pomiankowski A. Lane N. The origin of heredity in protocells Philos. Trans. R. Soc. Lond. B Biol. Sci. 2017 372 20160419 10.1098/rstb.2016.0419 29061892 PMC5665807 · DOI
  18. [31]Palmeira R.N. Colnaghi M. Harrison S.A. Pomiankowski A. Lane N. The limits of metabolic heredity in protocells Proc. R. Soc. B Biol. Sci. 2022 289 20221469 10.1098/rspb.2022.1469 36350219 PMC9653231 · DOI · Paper page
  19. [32]Aulakh S.K. Varma S.J. Ralser M. Metal ion availability and homeostasis as drivers of metabolic evolution and enzyme function Curr. Opin. Genet. Dev. 2022 77 101987 10.1016/j.gde.2022.101987 36183585 · DOI
  20. [33]Dupont C.L. Butcher A. Valas R.E. Bourne P.E. Caetano-Anollés G. History of biological metal utilization inferred through phylogenomic analysis of protein structures Proc. Natl. Acad. Sci. USA 2010 107 10567 10572 10.1073/pnas.0912491107 20498051 PMC2890839 · DOI · Paper page
  21. [34]Belmonte L. Mansy S. Metal Catalysts and the Origin of Life Elements 2016 12 413 418 10.2113/gselements.12.6.413 · DOI
  22. [35]Martin W.F. Carbon–Metal Bonds: Rare and Primordial in Metabolism Trends Biochem. Sci. 2019 44 807 818 10.1016/j.tibs.2019.04.010 31104860 · DOI
  23. [36]Paulus H. Biosynthesis of the Aspartate Family of Amino Acids Bacillus Subtilis and Other Gram-Positive Bacteria John Wiley & Sons, Ltd. Hoboken, NJ, USA 2014 237 267 10.1128/9781555818388.ch18 · DOI
  24. [37]Jander G. Joshi V. Aspartate-Derived Amino Acid Biosynthesis in Arabidopsis thaliana Arab. Book 2009 7 e0121 10.1199/tab.0121 PMC3243338 22303247 · DOI
  25. [38]White R.H. l-Aspartate Semialdehyde and a 6-Deoxy-5-ketohexose 1-Phosphate Are the Precursors to the Aromatic Amino Acids in Methanocaldococcus Jannaschii Biochemistry 2004 43 7618 7627 10.1021/bi0495127 15182204 · DOI
  26. [39]Pittard J. Yang J. Biosynthesis of the Aromatic Amino Acids EcoSal Plus 2008 3 10.1128/ecosalplus.3.6.1.8 26443741 · DOI
  27. [40]Haines R.J. Pendleton L.C. Eichler D.C. Argininosuccinate synthase: At the center of arginine metabolism Int. J. Biochem. Mol. Biol. 2010 2 8 23 PMC3074183 21494411
  28. [41]Cunin R. Glansdorff N. Piérard A. Stalon V. Biosynthesis and metabolism of arginine in bacteria Microbiol. Rev. 1986 50 314 352 10.1128/mr.50.3.314-352.1986 3534538 PMC373073 · DOI
  29. [42]Ouchi T. Tomita T. Horie A. Yoshida A. Takahashi K. Nishida H. Lassak K. Taka H. Mineki R. Fujimura T. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus Nat. Chem. Biol. 2013 9 277 283 10.1038/nchembio.1200 23434852 · DOI
  30. [43]Zhang Y. Morar M. Ealick S.E. Structural biology of the purine biosynthetic pathway Cell. Mol. Life Sci. 2008 65 3699 3724 10.1007/s00018-008-8295-8 18712276 PMC2596281 · DOI
  31. [44]Kappock T.J. Ealick S.E. Stubbe J. Modular evolution of the purine biosynthetic pathway Curr. Opin. Chem. Biol. 2000 4 567 572 10.1016/S1367-5931(00)00133-2 11006546 · DOI
  32. [45]Nasu S. Wicks F. Gholson R. L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase J. Biol. Chem. 1982 257 626 632 10.1016/S0021-9258(19)68239-6 7033218 · DOI
  33. [46]Chandler J. Gholson R. Scott T. Studies on the de novo biosynthesis of NAD in Escherichia coli I. Labelling patterns from precursors Biochim. Biophys. Acta Gen. Subj. 1970 222 523 526 10.1016/0304-4165(70)90145-5 4321550 · DOI
  34. [48]Bossi R.T. Negri A. Tedeschi G. Mattevi A. Structure of FAD-Bound l-Aspartate Oxidase: Insight into Substrate Specificity and Catalysis Biochemistry 2002 41 3018 3024 10.1021/bi015939r 11863440 · DOI
  35. [49]Goldford J.E. Smith H.B. Longo L.M. Wing B.A. McGlynn S.E. Continuity between ancient geochemistry and modern metabolism enabled by non-autocatalytic purine biosynthesis bioRxiv 2022 10.1101/2022.10.07.511356 · DOI
  36. [50]Lee J. Sperandio V. Frantz D.E. Longgood J. Camilli A. Phillips M.A. Michael A.J. An Alternative Polyamine Biosynthetic Pathway Is Widespread in Bacteria and Essential for Biofilm Formation in Vibrio cholerae J. Biol. Chem. 2009 284 9899 9907 10.1074/jbc.M900110200 19196710 PMC2665113 · DOI
  37. [51]White R.H. The Conversion of a Phenol to an Aniline Occurs in the Biochemical Formation of the 1-(4-Aminophenyl)-1-deoxy-d-ribitol Moiety in Methanopterin Biochemistry 2011 50 6041 6052 10.1021/bi200362w 21634403 · DOI
  38. [52]Cronan J.E. Littel K.J. Jackowski S. Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium J. Bacteriol. 1982 149 916 922 10.1128/jb.149.3.916-922.1982 7037743 PMC216478 · DOI
  39. [53]Wang Y. Xu H. White R.H. β-Alanine Biosynthesis in Methanocaldococcus jannaschii J. Bacteriol. 2014 196 2869 2875 10.1128/JB.01784-14 24891443 PMC4135672 · DOI
  40. [54]van Poelje P.D. Snell E.E. Pyruvoyl-Dependent Enzymes Annu. Rev. Biochem. 1990 59 29 59 10.1146/annurev.bi.59.070190.000333 2197977 · DOI
  41. [55]Diaz E. Anton D.L. Alkylation of an active-site cysteinyl residue during substrate-dependent inactivation of Escherichia coli S-adenosylmethionine decarboxylase Biochemistry 1991 30 4078 4081 10.1021/bi00230a037 2018773 · DOI
  42. [56]Kezmarsky N.D. Xu H. Graham D. White R.H. Identification and characterization of a l-tyrosine decarboxylase in Methanocaldococcus jannaschii Biochim. Biophys. Acta Gen. Subj. 2005 1722 175 182 10.1016/j.bbagen.2004.12.003 15715981 · DOI
  43. [57]Yokooji Y. Tomita H. Atomi H. Imanaka T. Pantoate Kinase and Phosphopantothenate Synthetase, Two Novel Enzymes Necessary for CoA Biosynthesis in the Archaea J. Biol. Chem. 2009 284 28137 28145 10.1074/jbc.M109.009696 19666462 PMC2788864 · DOI
  44. [58]von Delft F. Lewendon A. Dhanaraj V. Blundell T.L. Abell C. Smith A.G. The Crystal Structure of E. coli Pantothenate Synthetase Confirms It as a Member of the Cytidylyltransferase Superfamily Structure 2001 9 439 450 10.1016/S0969-2126(01)00604-9 11377204 · DOI
  45. [59]Lee C.-Y. Chen A.F. Immobilized Coenzymes and Derivatives The Pyridine Nucleotide Coenzymes Everse J. Anderson B. You K.-S. Academic Press Cambridge, MA, USA 1982 189 224 10.1016/b978-0-12-244750-1.50015-4 · DOI
  46. [60]Reitzer L. Biosynthesis of Glutamate, Aspartate, Asparagine, L-Alanine, and D-Alanine EcoSal Plus 2004 1 10.1128/ecosalplus.3.6.1.3 26443364 · DOI
  47. [61]Huber C. Wächtershäuser G. Primordial reductive amination revisited Tetrahedron Lett. 2003 44 1695 1697 10.1016/S0040-4039(02)02863-0 · DOI
  48. [62]Barge L.M. Flores E. Baum M.M. VanderVelde D.G. Russell M.J. Redox and pH gradients drive amino acid synthesis in iron oxyhydroxide mineral systems Proc. Natl. Acad. Sci. USA 2019 116 4828 4833 10.1073/pnas.1812098116 30804197 PMC6421445 · DOI · Paper page
  49. [63]Kitadai N. Nakamura R. Yamamoto M. Takai K. Yoshida N. Oono Y. Metals likely promoted protometabolism in early ocean alkaline hydrothermal systems Sci. Adv. 2019 5 eaav7848 10.1126/sciadv.aav7848 31223650 PMC6584212 · DOI
  50. [64]Nakada H.I. Weinhouse S. Non-Enzymatic Transamination With Glyoxylic Acid And Various Amino Acids J. Biol. Chem. 1953 204 831 836 10.1016/S0021-9258(18)66086-7 13117860 · DOI
  51. [65]Cabello J. Basilio C. Prajoux V. Plaza M. Non-enzymic transamination between ornithine and glyoxylate Arch. Biochem. Biophys. 1963 100 512 515 10.1016/0003-9861(63)90119-X 14017544 · DOI
  52. [66]Longenecker J.B. Snell E.E. The Comparative Activities of Metal Ions in Promoting Pyridoxal-catalyzed Reactions of Amino Acids1 J. Am. Chem. Soc. 2002 79 142 145 10.1021/ja01558a036 · DOI
  53. [67]Percudani R. Peracchi A. A genomic overview of pyridoxal-phosphate-dependent enzymes EMBO Rep. 2003 4 850 854 10.1038/sj.embor.embor914 12949584 PMC1326353 · DOI
  54. [68]Eliot A.C. Kirsch J.F. Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations Annu. Rev. Biochem. 2004 73 383 415 10.1146/annurev.biochem.73.011303.074021 15189147 · DOI
  55. [69]Meisch H.U. Hoffmann H. Reinle W. Vanadium catalysis in the nonenzymatic transamination of δ-aminolevulinic acid Z. Nat.Sect. C 1978 33 623 628 10.1515/znc-1978-9-1003 · DOI
  56. [70]Banks B.E.C. Diamantis A.A. Vernon C.A. 825. Transamination. Part II. The non-enzymic reactions between pyridoxamine and pyruvic acid and between pyridoxal and alanine J. Chem. Soc. 1961 67 4235 4247 10.1039/jr9610004235 · DOI
  57. [71]Zabinski R.F. Toney M.D. Metal Ion Inhibition of Nonenzymatic Pyridoxal Phosphate Catalyzed Decarboxylation and Transamination J. Am. Chem. Soc. 2000 123 193 198 10.1021/ja0026354 11456503 · DOI
  58. [72]Maltais T.R. VanderVelde D. LaRowe D.E. Goldman A.D. Barge L.M. Reactivity of Metabolic Intermediates and Cofactor Stability under Model Early Earth Conditions Orig. Life Evol. Biosph. 2020 50 35 55 10.1007/s11084-019-09590-9 31981046 · DOI
  59. [73]Yu L. Sivitz W.I. Oxaloacetate Mediates Mitochondrial Metabolism and Function Curr. Metab. Syst. Biol. 2020 7 11 23 10.2174/2213235X07666191008103247 · DOI
  60. [75]Mayer R.J. Moran J. Quantifying Reductive Amination in Nonenzymatic Amino Acid Synthesis Angew. Chem. Int. Ed. 2022 61 e202212237 10.1002/anie.202212237 PMC9828492 36121198 · DOI · Paper page
  61. [76]Sogin E.M. Puskás E. Dubilier N. Liebeke M. Marine Metabolomics: A Method for Nontargeted Measurement of Metabolites in Seawater by Gas Chromatography–Mass Spectrometry Msystems 2019 4 e00638-19 10.1128/mSystems.00638-19 31822601 PMC6906741 · DOI
  62. [77]Jámbor A. Molnár-Perl I. Amino acid analysis by high-performance liquid chromatography after derivatization with 9-fluorenylmethyloxycarbonyl chloride: Literature overview and further study J. Chromatogr. A 2009 1216 3064 3077 10.1016/j.chroma.2009.01.068 19215925 · DOI
  63. [78]Wang J. Huang Z.-H. Gage D.A. Watson J. Analysis of amino acids by gas chromatography—Flame ionization detection and gas chromatography—Mass spectrometry: Simultaneous derivatization of functional groups by an aqueous-phase chloroformate-mediated reaction J. Chromatogr. A 1994 663 71 78 10.1016/0021-9673(94)80497-4 8180658 · DOI
  64. [79]Yin J. Wei Y. Liu D. Hu Y. Lu Q. Ang E.L. Zhao H. Zhang Y. An extended bacterial reductive pyrimidine degradation pathway that enables nitrogen release from β-alanine J. Biol. Chem. 2019 294 15662 15671 10.1074/jbc.RA119.010406 31455636 PMC6816092 · DOI
  65. [80]Martin W.F. Russell M.J. On the origin of biochemistry at an alkaline hydrothermal vent Philos. Trans. R. Soc. B Biol. Sci. 2006 362 1887 1926 10.1098/rstb.2006.1881 PMC2442388 17255002 · DOI · Paper page
  66. [81]Sojo V. Herschy B. Whicher A. Camprubí E. Lane N. The Origin of Life in Alkaline Hydrothermal Vents Astrobiology 2016 16 181 197 10.1089/ast.2015.1406 26841066 · DOI · Paper page
  67. [82]Herschy B. Whicher A. Camprubi E. Watson C. Dartnell L. Ward J. Evans J.R.G. Lane N. An Origin-of-Life Reactor to Simulate Alkaline Hydrothermal Vents J. Mol. Evol. 2014 79 213 227 10.1007/s00239-014-9658-4 25428684 PMC4247476 · DOI · Paper page
  68. [83]Russell M.J. Hall A.J. The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front J. Geol. Soc. 1997 154 377 402 10.1144/gsjgs.154.3.0377 11541234 · DOI · Paper page
  69. [84]Asano T. Le Noble W.J. Activation and Reaction Volumes in Solution Chem. Rev. 1978 78 407 489 10.1021/cr60314a004 11848963 · DOI
  70. [85]Krebs H.A. The effect of inorganic salts on the ketone decomposition of oxaloacetic acid Biochem. J. 1942 36 303 305 10.1042/bj0360303 16747526 PMC1265695 · DOI
  71. [86]Ito H. Kobayashi H. Nomiya K. Metal-ion catalyzed decarboxylation of oxaloacetic acid J. Chem. Soc. Faraday Trans. 1 Phys. Chem. Condens. Phases 1973 69 113 121 10.1039/f19736900113 · DOI
  72. [87]Holland H.D. The Chemical Evolution of the Atmosphere and Oceans Princeton University Press Princeton, NJ, USA 2020 10.2307/j.ctv15r58kg · DOI
  73. [88]Jordan S.F. Nee E. Lane N. Isoprenoids enhance the stability of fatty acid membranes at the emergence of life potentially leading to an early lipid divide Interface Focus 2019 9 20190067 10.1098/rsfs.2019.0067 31641436 PMC6802135 · DOI · Paper page
  74. [89]Walton C.R. Rimmer P. Shorttle O. Can prebiotic systems survive in the wild? An interference chemistry approach Front. Earth Sci. 2022 10 1011717 10.3389/feart.2022.1011717 · DOI
  75. [90]Charlou J. Donval J. Fouquet Y. Jean-Baptiste P. Holm N. Geochemistry of high H2 and CH4 vent fluids issuing from ultramafic rocks at the Rainbow hydrothermal field (36°14′N, MAR) Chem. Geol. 2002 191 345 359 10.1016/S0009-2541(02)00134-1 · DOI
  76. [92]Fuchs G. Alternative Pathways of Carbon Dioxide Fixation: Insights into the Early Evolution of Life? Annu. Rev. Microbiol. 2011 65 631 658 10.1146/annurev-micro-090110-102801 21740227 · DOI · Paper page
  77. [93]Hudson R. de Graaf R. Rodin M.S. Ohno A. Lane N. McGlynn S.E. Yamada Y.M.A. Nakamura R. Barge L.M. Braun D. CO 2 reduction driven by a pH gradient Proc. Natl. Acad. Sci. USA 2020 117 22873 22879 10.1073/pnas.2002659117 32900930 PMC7502746 · DOI · Paper page
  78. [94]Raschle T. Arigoni D. Brunisholz R. Rechsteiner H. Amrhein N. Fitzpatrick T.B. Reaction Mechanism of Pyridoxal 5′-Phosphate Synthase. Detection of an enzyme-bound chromophoric intermediate J. Biol. Chem. 2007 282 6098 6105 10.1074/jbc.m610614200 17189272 · DOI
  79. [95]Camprubi E. Harrison S. Jordan S. Bonnel J. Pinna S. Lane N. Do Soluble Phosphates Direct the Formose Reaction towards Pentose Sugars? Astrobiology 2022 22 981 991 10.1089/ast.2021.0125 35833833 · DOI
  80. [96]Kopetzki D. Antonietti M. Hydrothermal formose reaction New J. Chem. 2011 35 1787 1794 10.1039/c1nj20191c · DOI
  81. [97]Omran A. Plausibility of the Formose Reaction in Alkaline Hydrothermal Vent Environments Orig. Life Evol. Biosph. 2020 1 13 10.1007/s11084-020-09599-5 32749559 · DOI
  82. [98]Austin S.M. Waddell T.G. Prebiotic Synthesis of Vitamin B6-type Compounds Orig. Life Evol. Biosph. 1999 29 287 296 10.1023/A:1006532518221 10389266 · DOI

Cited by

Sorted by citations

Authors
Harrison, S. A., Webb, W. L., Rammu, H., & Lane, N.
Affiliations
University College London (GB)
Corresponding author
  • Harrison, Stuart A.
  • Lane, Nick
ORCID
Venue
Life
Publisher
MDPI AG
Published
2023-05-12
Volume
13
Issue
5
Pages
1177
ISSN
2075-1729 (ISSN-L)
DOI
10.3390/life13051177
PMC
PMC10221237
OpenAlex
W4376274365
Cited by
25
References
15
Citations by year
2026: 4 · 2025: 6 · 2024: 12 · 2023: 3
FWCI
2.91
Type
journal article
Language
en
Open access
Licence
Locations
  • Life (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Biotechnology and Biological Sciences Research Council (BB/V003542/1, 2089390)
Topics
  • Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
Keywords
aspartate synthesis, prebiotic chemistry, protometabolism, origin of life, oxaloacetate, pyridoxamine, copper catalysis, transamination, beta-alanine, amino group transfer, pyridoxal, metal ion catalysis, cofactors, amino acid synthesis

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