S-Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii: Identification of a Novel Family of Pyruvoyl Enzymes
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Published in | Journal of Bacteriology Vol. 182; no. 23; pp. 6667 - 6672 |
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Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S-Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli. ABSTRACT Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S -Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli . Despite spermidine concentrations in the Methanococcales that are several times higher than in E. coli , no AdoMet decarboxylase gene was recognized in the complete genome sequence of Methanococcus jannaschii . The gene encoding AdoMet decarboxylase in this archaeon is identified herein as a highly diverged homolog of the E. coli speD gene (less than 11% identity). The M. jannaschii enzyme has been expressed in E. coli and purified to homogeneity. Mass spectrometry showed that the enzyme is composed of two subunits of 61 and 63 residues that are derived from a common proenzyme; these proteins associate in an (αβ) 2 complex. The pyruvoyl-containing subunit is less than one-half the size of that in previously reported AdoMet decarboxylases, but the holoenzyme has enzymatic activity comparable to that of other AdoMet decarboxylases. The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet decarboxylases that includes homologs in other archaea and diverse bacteria. The broad phylogenetic distribution of this group suggests that the canonical SpeD-type decarboxylase was derived from an archaeal enzyme within the gamma proteobacterial lineage. Both SpeD-type and archaeal-type enzymes have diverged widely in sequence and size from analogous eucaryal enzymes. Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S-Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli. Despite spermidine concentrations in the Methanococcales that are several times higher than in E. coli, no AdoMet decarboxylase gene was recognized in the complete genome sequence of Methanococcus jannaschii. The gene encoding AdoMet decarboxylase in this archaeon is identified herein as a highly diverged homolog of the E. coli speD gene (less than 11% identity). The M. jannaschii enzyme has been expressed in E. coli and purified to homogeneity. Mass spectrometry showed that the enzyme is composed of two subunits of 61 and 63 residues that are derived from a common proenzyme; these proteins associate in an (alphabeta)(2) complex. The pyruvoyl-containing subunit is less than one-half the size of that in previously reported AdoMet decarboxylases, but the holoenzyme has enzymatic activity comparable to that of other AdoMet decarboxylases. The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet decarboxylases that includes homologs in other archaea and diverse bacteria. The broad phylogenetic distribution of this group suggests that the canonical SpeD-type decarboxylase was derived from an archaeal enzyme within the gamma proteobacterial lineage. Both SpeD-type and archaeal-type enzymes have diverged widely in sequence and size from analogous eucaryal enzymes. Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S -Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli . Despite spermidine concentrations in the Methanococcales that are several times higher than in E. coli , no AdoMet decarboxylase gene was recognized in the complete genome sequence of Methanococcus jannaschii . The gene encoding AdoMet decarboxylase in this archaeon is identified herein as a highly diverged homolog of the E. coli speD gene (less than 11% identity). The M. jannaschii enzyme has been expressed in E. coli and purified to homogeneity. Mass spectrometry showed that the enzyme is composed of two subunits of 61 and 63 residues that are derived from a common proenzyme; these proteins associate in an (αβ) 2 complex. The pyruvoyl-containing subunit is less than one-half the size of that in previously reported AdoMet decarboxylases, but the holoenzyme has enzymatic activity comparable to that of other AdoMet decarboxylases. The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet decarboxylases that includes homologs in other archaea and diverse bacteria. The broad phylogenetic distribution of this group suggests that the canonical SpeD-type decarboxylase was derived from an archaeal enzyme within the gamma proteobacterial lineage. Both SpeD-type and archaeal-type enzymes have diverged widely in sequence and size from analogous eucaryal enzymes. Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S-Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli. Despite spermidine concentrations in the Methanococcales that are several times higher than in Ecoli, no AdoMet decarboxylase gene was recognized in the complete genome sequence of Methanococcus jannaschii. The gene encoding AdoMet decarboxylase in this archaeon is identified herein as a highly diverged homolog of the E. coli speD gene (less than 11% identity). The M. jannaschii enzyme has been expressed in E. coli and purified to homogeneity. Mass spectrometry showed that the enzyme is composed of two subunits of 61 and 63 residues that are derived from a common proenzyme; these proteins associate in an ( alpha beta ) sub(2) complex. The pyruvoyl-containing subunit is less than one-half the size of that in previously reported AdoMet decarboxylases, but the holoenzyme has enzymatic activity comparable to that of other AdoMet decarboxylases. The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet decarboxylases that includes homologs in other archaea and diverse bacteria. The broad phylogenetic distribution of this group suggests that the canonical SpeD-type decarboxylase was derived from an archaeal enzyme within the gamma proteobacterial lineage. Both SpeD-type and archaeal-type enzymes have diverged widely in sequence and size from analogous eucaryal enzymes. |
Author | Alexander D. Kim David E. Graham George D. Markham Steven H. Seeholzer |
AuthorAffiliation | Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, 1 and Department of Microbiology, University of Illinois at Urbana- Champaign, Urbana, Illinois 61801 2 |
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Cites_doi | 10.1146/annurev.bi.59.070190.000333 10.1016/S1367-5931(97)80065-8 10.1128/jb.154.3.1315-1322.1983 10.1002/(SICI)1521-3773(20000204)39:3<450::AID-ANIE450>3.0.CO;2-F 10.1146/annurev.bi.53.070184.003533 10.1146/annurev.pa.35.040195.000415 10.1007/BF02109483 10.1021/bi00230a037 10.1016/S0021-9258(18)61579-0 10.1038/nsb0498-289 10.1021/bi00256a013 10.1128/jb.171.8.4457-4465.1989 10.1074/jbc.274.49.35059 10.1042/bj1410581 10.1021/bi9825201 10.1128/MMBR.64.1.202-236.2000 10.1042/bst0260580 10.1042/bst0220863 10.1016/S0021-9258(18)33678-0 10.1016/0022-2836(85)90204-9 10.1093/nar/25.17.3389 10.1016/S0021-9258(17)40957-4 10.1093/nar/22.22.4673 10.1016/S0969-2126(99)80074-4 10.1074/jbc.275.6.4055 10.1126/science.273.5278.1058 10.1016/S0076-6879(96)66033-9 10.1046/j.1365-2958.2000.01930.x 10.1016/S0021-9258(18)63216-8 10.1111/j.1432-1033.1991.tb16136.x |
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Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Institute for Cancer Research, Fox Chase Cancer Center, 7701 Burholme Ave., Philadelphia, PA 19111. Phone: (215) 728-2439. Fax: (215) 728-3574. E-mail: GD_Markham@fccc.edu. |
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Mendeley... Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal... ABSTRACT Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and... |
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SubjectTerms | Adenosylmethionine Decarboxylase - classification Adenosylmethionine Decarboxylase - genetics Adenosylmethionine Decarboxylase - isolation & purification Adenosylmethionine Decarboxylase - metabolism Bacteria Bacteriology Base Sequence Binding Sites DNA, Archaeal Enzyme Precursors - metabolism Enzymes Enzymes and Proteins Escherichia coli - metabolism Methanococcales jannaschii Methanococcus - enzymology Methanococcus - genetics Methanococcus jannaschii Molecular Sequence Data Phylogeny Polyamines Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods speD gene |
Title | S-Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii: Identification of a Novel Family of Pyruvoyl Enzymes |
URI | http://jb.asm.org/content/182/23/6667.abstract https://www.ncbi.nlm.nih.gov/pubmed/11073910 https://www.proquest.com/docview/227064703 https://search.proquest.com/docview/17828299 https://search.proquest.com/docview/72404690 https://pubmed.ncbi.nlm.nih.gov/PMC111408 |
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