دورية أكاديمية

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

التفاصيل البيبلوغرافية
العنوان: S -Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii : Identification of a Novel Family of Pyruvoyl Enzymes
المؤلفون: Kim, Alexander D., Graham, David E., Seeholzer, Steven H., Markham, George D.
المصدر: Journal of Bacteriology ; volume 182, issue 23, page 6667-6672 ; ISSN 0021-9193 1098-5530
بيانات النشر: American Society for Microbiology
سنة النشر: 2000
الوصف: 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.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1128/jb.182.23.6667-6672.2000
DOI: 10.1128/JB.182.23.6667-6672.2000
الإتاحة: https://doi.org/10.1128/jb.182.23.6667-6672.2000Test
حقوق: https://journals.asm.org/non-commercial-tdm-licenseTest
رقم الانضمام: edsbas.B0557B0B
قاعدة البيانات: BASE