Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93

Kim, Keehyuk; Plapp, Bryce V.

doi:10.1016/j.cbi.2016.12.016

Title: Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93

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Authors:

; Plapp, Bryce V.

Publication Date:: 2017-10-01

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

OSTI Identifier:: 1550642

Grant/Contract Number:: AC02-CH11231; AC02-06CH11357

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: Chemico-Biological Interactions

Additional Journal Information:: Journal Name: Chemico-Biological Interactions Journal Volume: 276 Journal Issue: C; Journal ID: ISSN 0009-2797

Publisher:: Elsevier

Country of Publication:: Netherlands

Language:: English

Citation Formats


                    Kim, Keehyuk, and Plapp, Bryce V. Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93.  Netherlands: N. p., 2017. 
Web.  doi:10.1016/j.cbi.2016.12.016.

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                    Kim, Keehyuk, & Plapp, Bryce V. Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93.  Netherlands.  https://doi.org/10.1016/j.cbi.2016.12.016

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                    Kim, Keehyuk, and Plapp, Bryce V. Sun .  
"Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93".  Netherlands.  https://doi.org/10.1016/j.cbi.2016.12.016.

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@article{osti_1550642,

  title        = {Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93},

  author       = {Kim, Keehyuk and Plapp, Bryce V.},

  abstractNote = {},

  doi          = {10.1016/j.cbi.2016.12.016},

  journal      = {Chemico-Biological Interactions},

  number       = C,

  volume       = 276,

  place        = {Netherlands},

  year         = {2017},

  month        = {10}

}

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https://doi.org/10.1016/j.cbi.2016.12.016

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Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93

Journal Article Kim, Keehyuk ; Plapp, Bryce V. - Chemico-Biological Interactions

The substrate specificities of alcohol dehydrogenases (ADH) are of continuing interest for understanding the physiological functions of these enzymes. Ser-48 and Phe-93 have been identified as important residues in the substrate binding sites of ADHs, but more comprehensive structural and kinetic studies are required. The S48T substitution in horse ADH1E has small effects on kinetic constants and catalytic efficiency (V/Km) with ethanol, but decreases activity with benzyl alcohol and affinity for 2,2,2-trifluoroethanol (TFE) and 2,3,4,5,6-pentafluorobenzyl alcohol (PFB). Nevertheless, atomic resolution crystal structures of the S48T enzyme complexed with NAD+ and TFE or PFB are very similar to the structures formore »« less
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Active site substituted Co(II)-, Ni(II)-, and Cd(II)-horse liver alcohol dehydrogenase derivatives are compared to the native Zn(II)-enzyme with respect to the kinetic properties associated with the formation and decay of the intermediate observed in the reaction of the binary E-(NADH) complex with the intense substrate chromophore trans-4-(N,N-dimethylamino) cinnamaldehyde (DACA), lambda/sub max/ 398 nm (H/sub 2/O). All the metal ion subsituted enzymes were found to form intermediates with red-shifted spectra upon reaction with DACA and NADH. The magnitudes of (1) the red shifts, (2) the specific rate constants (k/sub off/) for dissociation of DACA from the intermediate, and (3) the hydridemore »« less
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