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Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli
SpringerPlus
  • Wade C. McGregor, Arizona State University
  • Danuta Gillner, Loyola University Chicago
  • Sabina I. Swierczek, Marquette University
  • Dali Liu, Loyola University Chicago
  • Richard C. Holz, Marquette University
Document Type
Article
Publication Date
1-1-2013
Disciplines
Abstract
The H355A, H355K, H80A, and H80K mutant enzymes of the argE-encoded N-acetyl-L-ornithine deacetylase (ArgE) from Escherichia coli were prepared, however, only the H355A enzyme was found to be soluble. Kinetic analysis of the Co(II)-loaded H355A exhibited activity levels that were 380-fold less than Co(II)-loaded WT ArgE. Electronic absorption spectra of Co(II)-loaded H355A-ArgE indicate that the bound Co(II) ion resides in a distorted, five-coordinate environment and Isothermal Titration Calorimetry (ITC) data for Zn(II) binding to the H355A enzyme provided a dissociation constant (Kd) of 39 μM. A three-dimensional homology model of ArgE was generated using the X-ray crystal structure of the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae confirming the assignment of H355 as well as H80 as active site ligands.
Comments

Published version. SpringerPlus, Vol. 2 (2013): 482-491. DOI. © 2013 McGregor et al.; licensee Springer. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.

Citation Information
Wade C. McGregor, Danuta Gillner, Sabina I. Swierczek, Dali Liu, et al.. "Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli" SpringerPlus (2013) ISSN: 2193-1801
Available at: http://works.bepress.com/richard_holz/97/