ArticleThe Journal of biological chemistry2007
Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 66 citations in OpenAlex.
- Mutational and Functional Analyses of Substrate Binding and Catalysis of theBiochemistry · 2020Article
- A New Class of EutT ATP:Co(I)rrinoid Adenosyltransferases Found in Listeria monocytogenes and Other Firmicutes Does Not Require a Metal Ion for Activity.Biochemistry · 2018Article
- Harnessing self-assembled peptide nanoparticles in epitope vaccine design.Biotechnology advances · 2017Review
- Article
- Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co(I)rrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co(II)rrinoids.Angewandte Chemie (International ed. in English) · 2015Article
- Spectroscopic studies of the Salmonella enterica adenosyltransferase enzyme SeCobA: molecular-level insight into the mechanism of substrate Cob(II)alamin activation.Biochemistry · 2014Article
- Diverse bacterial microcompartment organelles.Microbiology and molecular biology reviews : MMBR · 2014Review
- the Eutt enzyme of Salmonella enterica is a unique ATP:Cob(I)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity.Journal of bacteriology · 2014Article
- Spectroscopic characterization of active-site variants of the PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri: insights into the mechanism of four-coordinate Co(II)corrinoid formation.Inorganic chemistry · 2012Article
- Loss of allostery and coenzyme B12 delivery by a pathogenic mutation in adenosyltransferase.Biochemistry · 2011Article
- Genetic disorders of vitamin B₁₂ metabolism: eight complementation groups--eight genes.Expert reviews in molecular medicine · 2010Review
- Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment.Journal of bacteriology · 2010Article
- Functional and structural analysis of five mutations identified in methylmalonic aciduria cblB type.Human mutation · 2010Article
- Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12.Applied microbiology and biotechnology · 2010Review
- Vitamin B12: unique metalorganic compounds and the most complex vitamins.Molecules (Basel, Switzerland) · 2010Review
- Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?The Journal of biological chemistry · 2010Article
- An investigation of the catalytic mechanism of S-adenosylmethionine synthetase by QM/MM calculations.Archives of biochemistry and biophysics · 2009Article
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- Article
- Crystallization and preliminary X-ray crystallographic studies of a PduO-type ATP:cob(I)alamin adenosyltransferase from Bacillus cereus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The three-dimensional crystal structure of the PduO-type corrinoid adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to 1.68-A resolution. The functional assignment of LrPduO as a corrinoid adenosyltransferase was confirmed by in vivo and in vitro evidence. The enzyme has an apparent Km(ATP) of 2.2 microM and Km(Cobalamin) of 0.13 microM and a kcat of 0.025 s(-1). Co-crystallization of the enzyme with Mg-ATP resulted in well-defined electron density for an N-terminal loop that had been disordered in other PduO-type enzyme structures. This newly defined N-terminal loop makes up the lower portion of the enzyme active site with the other half being contributed from an adjacent subunit. These results provide the first detailed description of the enzyme active site for a PduO-type adenosyltransferase and identify a unique ATP binding motif at the protein N terminus. The molecular architecture at the active site offers valuable new insight into the role of various residues responsible for the human disease methylmalonic aciduria.
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