Open Access. Powered by Scholars. Published by Universities.®
- Discipline
Articles 1 - 4 of 4
Full-Text Articles in Physics
Slow-Binding Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By Peptide Thiols: Synthesis And Spectroscopic Characterization, Kristi M. Huntington, David L. Bienvenue, Yaoming Wei, Brian Bennett, Richard C. Holz, Dehua Pei
Slow-Binding Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By Peptide Thiols: Synthesis And Spectroscopic Characterization, Kristi M. Huntington, David L. Bienvenue, Yaoming Wei, Brian Bennett, Richard C. Holz, Dehua Pei
Physics Faculty Research and Publications
Peptide-derived thiols of the general structure N-mercaptoacyl-leucyl-p-nitroanilide (1a−c) were synthesized and found to be potent, slow-binding inhibitors of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potencies (KI*) of these inhibitors against AAP range from 2.5 to 57 nM exceeding that of the natural product bestatin and approaching that of amastatin. The corresponding alcohols (2a−b) are simple competitive inhibitors of much lower potencies (KI = 23 and 360 μM). These data suggest that the free thiols are involved in the formation of the E·I …
Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By Aliphatic Alcohols. Characterization Of The Hydrophobic Substrate Recognition Site, Leila Ustynyuk, Brian Bennett, Tanya Edwards, Richard C. Holz
Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By Aliphatic Alcohols. Characterization Of The Hydrophobic Substrate Recognition Site, Leila Ustynyuk, Brian Bennett, Tanya Edwards, Richard C. Holz
Physics Faculty Research and Publications
Seven aliphatic and two aromatic alcohols were tested as reporters of the substrate selectivity of the aminopeptidase from Aeromonas proteolytica (AAP). This series of alcohols was chosen to systematically probe the effect of carbon chain length, steric bulk, and inhibitor shape on the inhibition of AAP. Initially, however, the question of whether AAP is denatured in the presence of aliphatic alcohols was addressed. On the basis of circular dichroism (CD), electronic absorption, and fluorescence spectra, the secondary structure of AAP, with and without added aliphatic alcohols, was unchanged. These data clearly indicate that AAP is not denatured in aliphatic alcohols, …
1-Butaneboronic Acid Binding To Aeromonas Proteolytica Aminopeptidase: A Case Of Arrested Development, Carin C. De Paola, Brian Bennett, Richard C. Holz, Dagmar Ringe, Gregory A. Petsko
1-Butaneboronic Acid Binding To Aeromonas Proteolytica Aminopeptidase: A Case Of Arrested Development, Carin C. De Paola, Brian Bennett, Richard C. Holz, Dagmar Ringe, Gregory A. Petsko
Physics Faculty Research and Publications
Hydrolases containing two metal ions connected by a bridging ligand catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical pathways, and protein degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm for the study of such bridged bimetallic proteases since its three-dimensional structure is known to very high resolution and its catalytic reaction is amenable to spectroscopic examination. Herein, we report the X-ray crystal structure at 1.9 Å resolution of AAP complexed with 1-butaneboronic acid (BuBA). This structure suggests that this complex represents a snapshot of the proteolytic reaction in an arrested form between …
Models For Molybdenum Coordination During The Catalytic Cycle Of Periplasmic Nitrate Reductase From Paracoccus Denitrificans Derived From Epr And Exafs Spectroscopy, Clive S. Butler, John M. Charnock, Brian Bennett, Heather J. Sears, Ann J. Reilly, Stuart J. Ferguson, C. David Garner, David J. Lowe, Andrew J. Thomson, Ben C. Berks, David J. Richardson
Models For Molybdenum Coordination During The Catalytic Cycle Of Periplasmic Nitrate Reductase From Paracoccus Denitrificans Derived From Epr And Exafs Spectroscopy, Clive S. Butler, John M. Charnock, Brian Bennett, Heather J. Sears, Ann J. Reilly, Stuart J. Ferguson, C. David Garner, David J. Lowe, Andrew J. Thomson, Ben C. Berks, David J. Richardson
Physics Faculty Research and Publications
The periplasmic nitrate reductase from Paracoccus denitrificans is a soluble two-subunit enzyme which binds two hemes (c-type), a [4Fe-4S] center, and a bis molybdopterin guanine dinucleotide cofactor (bis-MGD). A catalytic cycle for this enzyme is presented based on a study of these redox centers using electron paramagnetic resonance (EPR) and extended X-ray absorption fine structure (EXAFS) spectroscopies. The Mo(V) EPR signal of resting NAP (High g [resting]) has gav = 1.9898 is rhombic, exhibits low anisotropy, and is split by two weakly interacting protons which are not solvent-exchangeable. Addition of exogenous ligands to this resting …