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McGregor WC, Gillner DM, Swierczek SI, et al. Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli. Springerplus. 2013;2:482doi: 10.1186/2193-1801-2-482.
McGregor, W. C., Gillner, D. M., Swierczek, S. I., Liu, D., & Holz, R. C. (2013). Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli. SpringerPlus, 2482. https://doi.org/10.1186/2193-1801-2-482
McGregor, Wade C, et al. "Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli." SpringerPlus vol. 2 (2013): 482. doi: https://doi.org/10.1186/2193-1801-2-482
McGregor WC, Gillner DM, Swierczek SI, Liu D, Holz RC. Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli. Springerplus. 2013 Sep 23;2:482. doi: 10.1186/2193-1801-2-482. eCollection 2013. PMID: 25674394; PMCID: PMC4320195.
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Springerplus. 2013 Sep 23;2:482. doi: 10.1186/2193-1801-2-482. eCollection 2013.

Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli.

SpringerPlus

Wade C McGregor, Danuta M Gillner, Sabina I Swierczek, Dali Liu, Richard C Holz

Affiliations

  1. The Department of Applied Sciences and Mathematics, College of Technology and Innovation, Arizona State University, Mesa, AZ 85212 USA.
  2. Chemistry and Biochemistry, Loyola University Chicago, Chicago, IL 60626 USA ; The Department of Chemistry, Silesian University of Technology, Gliwice, 44-100 Poland.
  3. Contribution from the Department of Chemistry, Marquette University, Milwaukee, WI 53233 USA.
  4. Chemistry and Biochemistry, Loyola University Chicago, Chicago, IL 60626 USA.
  5. Contribution from the Department of Chemistry, Marquette University, Milwaukee, WI 53233 USA ; Chemistry and Biochemistry, Loyola University Chicago, Chicago, IL 60626 USA.

PMID: 25674394 PMCID: PMC4320195 DOI: 10.1186/2193-1801-2-482

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 (K d) 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.

Keywords: Active site ligands; Bioinorganic Chemistry; Deacetylase; Hydrolysis; Isothermal titration calorimetry; Mechanistic enzymology; Zinc

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