Year |
Citation |
Score |
2018 |
Grell TAJ, Bell BN, Nguyen C, Dowling DP, Bruender NA, Bandarian V, Drennan CL. Crystal structure of AdoMet radical enzyme 7-carboxy-7-deazaguanine synthase from Escherichia coli suggests how modifications near [4Fe-4S] cluster engender flavodoxin specificity. Protein Science : a Publication of the Protein Society. PMID 30341796 DOI: 10.2210/Pdb6Nhl/Pdb |
0.554 |
|
2018 |
Grell TAJ, Kincannon WM, Bruender NA, Blaesi EJ, Krebs C, Bandarian V, Drennan CL. Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. The Journal of Biological Chemistry. PMID 30217813 DOI: 10.1074/Jbc.Ra118.005369 |
0.569 |
|
2018 |
Lewis JK, Bruender NA, Bandarian V. QueE: A Radical SAM Enzyme Involved in the Biosynthesis of 7-Deazapurine Containing Natural Products. Methods in Enzymology. 606: 95-118. PMID 30097106 DOI: 10.1016/Bs.Mie.2018.05.001 |
0.51 |
|
2018 |
Kincannon W, Bruender NA, Bandarian V. A Radical Clock Probe Uncouples H-atom Abstraction from Thi-oether Crosslink Formation by the Radical SAM Enzyme SkfB. Biochemistry. PMID 29965747 DOI: 10.1021/Acs.Biochem.8B00537 |
0.471 |
|
2018 |
Wilcoxen J, Bruender NA, Bandarian V, Britt RD. A Radical Intermediate in Bacillus subtilis QueE During Turnover With the Substrate Analog 6-Carboxypterin. Journal of the American Chemical Society. PMID 29303575 DOI: 10.1021/Jacs.7B10860 |
0.496 |
|
2017 |
Bruender NA, Bandarian V. The creatininase homolog MftE from Mycobacterium smegmatis catalyzes a peptide cleavage reaction in the biosynthesis of a novel RiPP. The Journal of Biological Chemistry. PMID 28077628 DOI: 10.1074/Jbc.M116.762062 |
0.443 |
|
2017 |
Bruender NA, Grell TA, Dowling DP, McCarty RM, Drennan CL, Bandarian V. 7-Carboxy-7-deazaguanine synthase - A radical S-adenosyl-L-methionine enzyme with polar tendencies. Journal of the American Chemical Society. PMID 28045519 DOI: 10.1021/Jacs.6B11381 |
0.524 |
|
2016 |
Bruender NA, Bandarian V. SkfB abstracts a hydrogen atom from Cα on SkfA to initiate thioether crosslink formation. Biochemistry. PMID 27410522 DOI: 10.1021/Acs.Biochem.6B00598 |
0.44 |
|
2016 |
Bruender NA, Bandarian V. The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide. Biochemistry. PMID 27158836 DOI: 10.1021/Acs.Biochem.6B00355 |
0.489 |
|
2016 |
Bruender NA, Wilcoxen J, Britt RD, Bandarian V. Biochemical and spectroscopic characterization of a radical SAM enzyme involved in the formation of a peptide thioether crosslink. Biochemistry. PMID 27007615 DOI: 10.1021/Acs.Biochem.6B00145 |
0.448 |
|
2016 |
Bruender NA, Young AP, Bandarian V. Correction to Chemical and Biological Reduction of the Radical SAM Enzyme 7-Carboxy-7-deazaguanine Synthase. Biochemistry. PMID 26950390 DOI: 10.1021/Acs.Biochem.6B00147 |
0.462 |
|
2015 |
Bruender NA, Young AP, Bandarian V. Chemical and Biological Reduction of the Radical SAM Enzyme CPH4 Synthase. Biochemistry. 54: 2903-10. PMID 25933252 DOI: 10.1021/Acs.Biochem.5B00210 |
0.503 |
|
2014 |
Dowling DP, Bruender NA, Young AP, McCarty RM, Bandarian V, Drennan CL. Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism. Nature Chemical Biology. 10: 106-12. PMID 24362703 DOI: 10.1038/Nchembio.1426 |
0.526 |
|
2013 |
Thoden JB, Branch MC, Zimmer AL, Bruender NA, Holden HM. Active site architecture of a sugar N-oxygenase. Biochemistry. 52: 3191-3. PMID 23621882 DOI: 10.1021/Bi400407X |
0.548 |
|
2012 |
Bruender NA, Holden HM. Probing the catalytic mechanism of a C-3'-methyltransferase involved in the biosynthesis of D-tetronitrose. Protein Science : a Publication of the Protein Society. 21: 876-86. PMID 22495991 DOI: 10.1002/Pro.2074 |
0.62 |
|
2010 |
Bruender NA, Thoden JB, Kaur M, Avey MK, Holden HM. Molecular architecture of a C-3'-methyltransferase involved in the biosynthesis of D-tetronitrose. Biochemistry. 49: 5891-8. PMID 20527922 DOI: 10.1021/Bi100782B |
0.592 |
|
2010 |
Bruender NA, Thoden JB, Holden HM. X-ray structure of kijd3, a key enzyme involved in the biosynthesis of D-kijanose. Biochemistry. 49: 3517-24. PMID 20334431 DOI: 10.1021/Bi100318V |
0.62 |
|
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