Kinetic properties of mAMCase catalytic domain at various pH

This directory contains all files required to analyze the mouse AMCase enzyme kinetics across pH 2.0 to 8.0 presented in Figure 1 and Supplemental Figures 1 and 2 the manuscript Díaz et al., bioRxiv (2023).

Enzyme kinetics were performed using a Tecan Spark multimode microplate reader and data was analyzed using Graphpad Prism. Figures were compiled using Adobe Illustrator.

Files included in this directory:

20210906 - mAMCase_CatD_6xHis (pmRED006)

- 20210907 - Purification contains FPLC chromatograms and corresponding SDS-PAGE gel stained with InstantBlue.

- 202110XX _pHX_100nM contains four replicates performed at that specific pH using 100 nM mAMCase.

- 384w_exp.toml contains a 384-well plate layout of the experimental conditions. This file is compatible with wellmap.

- 384w_std.toml contains a 384-well plate layout of the 4MU standards. This file is compatible with wellmap.

Figures
- contains PDFs of V_max, k_cat, K_M, catalytic efficiency, and the initial rate for all pH points tested. 

20210906 - mAMCase_CatD_6xHis (pmRED006) - Data.pzfx

- contains all data from 20210906 - mAMCase_CatD_6xHis (pmRED006), including standard curves, initial time points, and initial rates curves. 

20210906 - mAMCase_CatD_6xHis (pmRED006) - Summary.pzfx

- contains summary data of kinetic parameters V_max, k_cat, K_M, catalytic efficiency, and initial rates for all pH points tested.

Contact:
Roberto Efraín Díaz, robertoefrain.diaz@ucsf.edu

James Fraser, jfraser@fraserlab.com