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Full-Text Articles in Physics
X-Ray Crystallographic Characterization Of The Co(Ii)-Substituted Tris-Bound Form Of The Aminopeptidase From Aeromonas Proteolytica, Petra Munih, Aaron Moulin, Carin Stamper, Brian Bennett, Dagmar Ringe, Gregory A. Petsko, Richard C. Holz
X-Ray Crystallographic Characterization Of The Co(Ii)-Substituted Tris-Bound Form Of The Aminopeptidase From Aeromonas Proteolytica, Petra Munih, Aaron Moulin, Carin Stamper, Brian Bennett, Dagmar Ringe, Gregory A. Petsko, Richard C. Holz
Physics Faculty Research and Publications
The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2 Å resolution. [CoCo(AAP)] folds into an α/β globular domain with a twisted β-sheet hydrophobic core sandwiched between α-helices, identical to [ZnZn(AAP)]. Co(II) binding to AAP does not introduce any major conformational changes to the overall protein structure and the amino acid residues ligated to the dicobalt(II) cluster in [CoCo(AAP)] are the same as those in the native Zn(II)-loaded structure with only minor perturbations in bond lengths. The Co(II)–Co(II) distance is 3.3 Å. Tris(hydroxymethyl)aminomethane (Tris) coordinates to the dinuclear Co(II) active site …
Experimental Evidence For A Metallohydrolase Mechanism In Which The Nucleophile Is Not Delivered By A Metal Ion: Epr Spectrokinetic And Structural Studies Of Aminopeptidase From Vibrio Proteolyticus, Amit Kumar, Gopal R. Periyannan, Aaron W. Kittell, Jung Ja Kim, Brian Bennett
Experimental Evidence For A Metallohydrolase Mechanism In Which The Nucleophile Is Not Delivered By A Metal Ion: Epr Spectrokinetic And Structural Studies Of Aminopeptidase From Vibrio Proteolyticus, Amit Kumar, Gopal R. Periyannan, Aaron W. Kittell, Jung Ja Kim, Brian Bennett
Physics Faculty Research and Publications
Metallohydrolases catalyse some of the most important reactions in biology and are targets for numerous chemotherapeutic agents designed to combat bacterial infectivity, antibiotic resistance, HIV infectivity, tumour growth, angiogenesis and immune disorders. Rational design of inhibitors of these enzymes with chemotherapeutic potential relies on detailed knowledge of the catalytic mechanism. The roles of the catalytic transition ions in these enzymes have long been assumed to include the activation and delivery of a nucleophilic hydroxy moiety. In the present study, catalytic intermediates in the hydrolysis of L-leucyl-L-leucyl-L-leucine by Vibrio proteolyticus aminopeptidase were characterized in spectrokinetic and structural studies. Rapid-freeze-quench EPR studies …