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Evidence of a sequestered imine intermediate during reduction of nitrile to amine by the nitrile reductase QueF from Escherichia coli.

Jung J, Nidetzky B.

J Biol Chem. 2018 Mar 9;293(10):3720-3733. doi: 10.1074/jbc.M117.804583. Epub 2018 Jan 16.


Pursuit of Noncovalent Interactions for Strategic Site-Selective Catalysis.

Toste FD, Sigman MS, Miller SJ.

Acc Chem Res. 2017 Mar 21;50(3):609-615. doi: 10.1021/acs.accounts.6b00613.


Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.

Kulkarni YS, Liao Q, Petrović D, Krüger DM, Strodel B, Amyes TL, Richard JP, Kamerlin SCL.

J Am Chem Soc. 2017 Aug 2;139(30):10514-10525. doi: 10.1021/jacs.7b05576. Epub 2017 Jul 19.


Metal Fluorides: Tools for Structural and Computational Analysis of Phosphoryl Transfer Enzymes.

Jin Y, Molt RW Jr, Blackburn GM.

Top Curr Chem (Cham). 2017 Apr;375(2):36. doi: 10.1007/s41061-017-0130-y. Epub 2017 Mar 15. Review.


Diversity of Secondary Structure in Catalytic Peptides with β-Turn-Biased Sequences.

Metrano AJ, Abascal NC, Mercado BQ, Paulson EK, Hurtley AE, Miller SJ.

J Am Chem Soc. 2017 Jan 11;139(1):492-516. doi: 10.1021/jacs.6b11348. Epub 2016 Dec 28.


Proteomic profile of the Bradysia odoriphaga in response to the microbial secondary metabolite benzothiazole.

Zhao Y, Cui K, Xu C, Wang Q, Wang Y, Zhang Z, Liu F, Mu W.

Sci Rep. 2016 Nov 24;6:37730. doi: 10.1038/srep37730.


Enzyme Catalysis To Power Micro/Nanomachines.

Ma X, Hortelão AC, Patiño T, Sánchez S.

ACS Nano. 2016 Oct 25;10(10):9111-9122. doi: 10.1021/acsnano.6b04108. Epub 2016 Oct 3.


Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.

Lopez-Zavala AA, Carrasco-Miranda JS, Ramirez-Aguirre CD, López-Hidalgo M, Benitez-Cardoza CG, Ochoa-Leyva A, Cardona-Felix CS, Diaz-Quezada C, Rudiño-Piñera E, Sotelo-Mundo RR, Brieba LG.

Biochim Biophys Acta. 2016 Dec;1864(12):1696-1706. doi: 10.1016/j.bbapap.2016.09.002. Epub 2016 Sep 7.


Conformational Sub-states and Populations in Enzyme Catalysis.

Agarwal PK, Doucet N, Chennubhotla C, Ramanathan A, Narayanan C.

Methods Enzymol. 2016;578:273-97. doi: 10.1016/bs.mie.2016.05.023. Epub 2016 Jul 9. Review.


Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.

Richard JP, Amyes TL, Malabanan MM, Zhai X, Kim KJ, Reinhardt CJ, Wierenga RK, Drake EJ, Gulick AM.

Biochemistry. 2016 May 31;55(21):3036-47. doi: 10.1021/acs.biochem.6b00311. Epub 2016 May 17.


Whither Enzymology in the Twenty First Century?

Marsh EN.

Front Chem. 2016 Apr 22;4:20. doi: 10.3389/fchem.2016.00020. eCollection 2016. No abstract available.


Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.

Lara-Gonzalez S, Estrella P, Portillo C, Cruces ME, Jimenez-Sandoval P, Fattori J, Migliorini-Figueira AC, Lopez-Hidalgo M, Diaz-Quezada C, Lopez-Castillo M, Trasviña-Arenas CH, Sanchez-Sandoval E, Gómez-Puyou A, Ortega-Lopez J, Arroyo R, Benítez-Cardoza CG, Brieba LG.

PLoS One. 2015 Nov 30;10(11):e0141747. doi: 10.1371/journal.pone.0141747. eCollection 2015.


Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.

Zhai X, Amyes TL, Richard JP.

J Am Chem Soc. 2015 Dec 9;137(48):15185-97. doi: 10.1021/jacs.5b09328. Epub 2015 Nov 30.


Structural effects of protein aging: terminal marking by deamidation in human triosephosphate isomerase.

de la Mora-de la Mora I, Torres-Larios A, Enríquez-Flores S, Méndez ST, Castillo-Villanueva A, Gómez-Manzo S, López-Velázquez G, Marcial-Quino J, Torres-Arroyo A, García-Torres I, Reyes-Vivas H, Oria-Hernández J.

PLoS One. 2015 Apr 17;10(4):e0123379. doi: 10.1371/journal.pone.0123379. eCollection 2015.


Transition States and transition state analogue interactions with enzymes.

Schramm VL.

Acc Chem Res. 2015 Apr 21;48(4):1032-9. doi: 10.1021/acs.accounts.5b00002. Epub 2015 Apr 7.


Experimental characterization of adsorbed protein orientation, conformation, and bioactivity.

Thyparambil AA, Wei Y, Latour RA.

Biointerphases. 2015 Mar 30;10(1):019002. doi: 10.1116/1.4906485.


An ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction.

Schiebel J, Chang A, Merget B, Bommineni GR, Yu W, Spagnuolo LA, Baxter MV, Tareilus M, Tonge PJ, Kisker C, Sotriffer CA.

Biochemistry. 2015 Mar 17;54(10):1943-55. doi: 10.1021/bi5014358. Epub 2015 Mar 3.


Enzyme dynamics from NMR spectroscopy.

Palmer AG 3rd.

Acc Chem Res. 2015 Feb 17;48(2):457-65. doi: 10.1021/ar500340a. Epub 2015 Jan 9. Review.


Extreme electric fields power catalysis in the active site of ketosteroid isomerase.

Fried SD, Bagchi S, Boxer SG.

Science. 2014 Dec 19;346(6216):1510-4. doi: 10.1126/science.1259802.


Reflections on the catalytic power of a TIM-barrel.

Richard JP, Zhai X, Malabanan MM.

Bioorg Chem. 2014 Dec;57:206-12. doi: 10.1016/j.bioorg.2014.07.001. Epub 2014 Jul 11.

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