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2018 | 2 |
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2020 | 3 |
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Characterization of a Unique Interrupted Adenylation Domain That Can Catalyze Three Reactions.
ACS Chem Biol. 2020 Jan 17;15(1):282-289. doi: 10.1021/acschembio.9b00929. Epub 2019 Dec 30.
ACS Chem Biol. 2020.
PMID: 31887013
A thorough analysis and categorization of bacterial interrupted adenylation domains, including previously unidentified families.
Lundy TA, Mori S, Garneau-Tsodikova S.
Lundy TA, et al.
RSC Chem Biol. 2020 Aug 18;1(4):233-250. doi: 10.1039/d0cb00092b. eCollection 2020 Oct 1.
RSC Chem Biol. 2020.
PMID: 34458763
Free PMC article.
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Engineering Bifunctional Enzymes Capable of Adenylating and Selectively Methylating the Side Chain or Core of Amino Acids.
Lundy TA, Mori S, Garneau-Tsodikova S.
Lundy TA, et al.
ACS Synth Biol. 2018 Feb 16;7(2):399-404. doi: 10.1021/acssynbio.7b00426. Epub 2018 Feb 2.
ACS Synth Biol. 2018.
PMID: 29393631
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Lessons learned in engineering interrupted adenylation domains when attempting to create trifunctional enzymes from three independent monofunctional ones.
Lundy TA, Mori S, Garneau-Tsodikova S.
Lundy TA, et al.
RSC Adv. 2020 Sep 15;10(56):34299-34307. doi: 10.1039/d0ra05490a. eCollection 2020 Sep 10.
RSC Adv. 2020.
PMID: 35519055
Free PMC article.
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Probing the limits of interrupted adenylation domains by engineering a trifunctional enzyme capable of adenylation, N-, and S-methylation.
Lundy TA, Mori S, Garneau-Tsodikova S.
Lundy TA, et al.
Org Biomol Chem. 2019 Jan 31;17(5):1169-1175. doi: 10.1039/c8ob02996b.
Org Biomol Chem. 2019.
PMID: 30644493
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Structural basis for backbone N-methylation by an interrupted adenylation domain.
Mori S, Pang AH, Lundy TA, Garzan A, Tsodikov OV, Garneau-Tsodikova S.
Mori S, et al. Among authors: lundy ta.
Nat Chem Biol. 2018 May;14(5):428-430. doi: 10.1038/s41589-018-0014-7. Epub 2018 Mar 19.
Nat Chem Biol. 2018.
PMID: 29556104
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