Alvan C. Hengge

Affiliations: 
Chemistry and Biochemistry Utah State University, Logan, UT, United States 
Area:
Organic Chemistry
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"Alvan Hengge"
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Publications

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Szeler K, Williams NH, Hengge AC, et al. (2020) Modeling the Alkaline Hydrolysis of Diaryl Sulfate Diesters: A Mechanistic Study. The Journal of Organic Chemistry
van Loo B, Berry R, Boonyuen U, et al. (2019) Transition-State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase. Biochemistry
Bigley AN, Xiang DF, Narindoshvili T, et al. (2019) Transition State Analysis of the Reaction Catalyzed by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry
Costa DMA, Gómez SV, de Araújo SS, et al. (2019) Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase. International Journal of Biological Macromolecules
Moise G, Morales Y, Beaumont V, et al. (2018) A YopH PTP1B Chimera shows the importance of WPD-loop sequence to activity, structure, and dynamics in protein tyrosine phosphatases. Biochemistry
Chu Y, Williams NH, Hengge AC. (2017) Transition States and Control of Substrate Preference in the Promiscuous Phosphatase PP1. Biochemistry
Coitinho JB, Pereira MS, Costa DM, et al. (2016) Structural and kinetic properties of the aldehyde dehydrogenase NahF, a broad substrate specificity enzyme for aldehyde oxidation. Biochemistry
Pereira MS, Murta B, Oliveira TC, et al. (2016) Mechanistic aspects of phosphate diester cleavage assisted by imidazole. A template reaction for obtaining aryl phosphoimidazoles. The Journal of Organic Chemistry
Moise G, Gallup NM, Alexandrova AN, et al. (2015) Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites. Biochemistry. 54: 6490-500
Hengge AC. (2015) Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases. Biochimica Et Biophysica Acta. 1854: 1768-75
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