S-Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii: Identification of a Novel Family of Pyruvoyl Enzymes

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Published inJournal of Bacteriology Vol. 182; no. 23; pp. 6667 - 6672
Main Authors Kim, A D, Graham, D E, Seeholzer, S H, Markham, G D
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.12.2000
Subjects
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
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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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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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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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StartPage 6667
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
Volume 182
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