ArticleThe Journal of biological chemistry2008
Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- The Pseudomonas aeruginosa Type VI secretion system toxin Tse8 evolved from a novel N-carbamoylputrescine amidohydrolase.The Biochemical journal · 2025Article
- Characterization of an Arginine Decarboxylase fromBiomolecules · 2024Article
- Functional polyamine metabolic enzymes and pathways encoded by the virosphere.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
- Comparative Genomic Analysis Reveals the Metabolism and Evolution of the Thermophilic Archaeal GenusFrontiers in microbiology · 2020Article
- Utilization of Phenol as Carbon Source by the Thermoacidophilic ArchaeonFrontiers in microbiology · 2020Article
- Polyamine function in archaea and bacteria.The Journal of biological chemistry · 2018Review
- Article
- Development of the Multiple Gene Knockout System with One-Step PCR in Thermoacidophilic CrenarchaeonArchaea (Vancouver, B.C.) · 2017Article
- Polyamines in Eukaryotes, Bacteria, and Archaea.The Journal of biological chemistry · 2016Review
- Augmenting the genetic toolbox for Sulfolobus islandicus with a stringent positive selectable marker for agmatine prototrophy.Applied and environmental microbiology · 2013Article
- Prediction and Analysis of Post-Translational Pyruvoyl Residue Modification Sites from Internal Serines in Proteins.PloS one · 2013Article
- Evolution and multiplicity of arginine decarboxylases in polyamine biosynthesis and essential role in Bacillus subtilis biofilm formation.The Journal of biological chemistry · 2010Article
- Molecular characterization of the Arginine decarboxylase gene family in rice.Transgenic research · 2010Article
- Pyridoxal 5'-phosphate: electrophilic catalyst extraordinaire.Current opinion in chemical biology · 2009Review
- An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae.The Journal of biological chemistry · 2009Article
- Outer and inner membrane proteins compose an arginine-agmatine exchange system in Chlamydophila pneumoniae.Journal of bacteriology · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The crenarchaeon Sulfolobus solfataricus uses arginine to produce putrescine for polyamine biosynthesis. However, genome sequences from S. solfataricus and most crenarchaea have no known homologs of the previously characterized pyridoxal 5'-phosphate or pyruvoyl-dependent arginine decarboxylases that catalyze the first step in this pathway. Instead they have two paralogs of the S-adenosylmethionine decarboxylase (AdoMetDC). The gene at locus SSO0585 produces an AdoMetDC enzyme, whereas the gene at locus SSO0536 produces a novel arginine decarboxylase (ArgDC). Both thermostable enzymes self-cleave at conserved serine residues to form amino-terminal beta-domains and carboxyl-terminal alpha-domains with reactive pyruvoyl cofactors. The ArgDC enzyme specifically catalyzed arginine decarboxylation more efficiently than previously studied pyruvoyl enzymes. alpha-Difluoromethylarginine significantly reduced the ArgDC activity of purified enzyme, and treating growing S. solfataricus cells with this inhibitor reduced the cells' ratio of spermidine to norspermine by decreasing the putrescine pool. The crenarchaeal ArgDC had no AdoMetDC activity, whereas its AdoMetDC paralog had no ArgDC activity. A chimeric protein containing the beta-subunit of SSO0536 and the alpha-subunit of SSO0585 had ArgDC activity, implicating residues responsible for substrate specificity in the amino-terminal domain. This crenarchaeal ArgDC is the first example of alternative substrate specificity in the AdoMetDC family. ArgDC activity has evolved through convergent evolution at least five times, demonstrating the utility of this enzyme and the plasticity of amino acid decarboxylases.
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