Zobrazeno 1 - 10
of 13
pro vyhledávání: '"David L Bienvenue"'
Autor:
Michelle L Scalley-Kim, Bruce W Hess, Ryan L Kelly, Anne-Rachel F Krostag, Kurt H Lustig, John S Marken, Pamela J Ovendale, Aaron R Posey, Pamela J Smolak, Janelle D L Taylor, C L Wood, David L Bienvenue, Peter Probst, Ruth A Salmon, Daniel S Allison, Teresa M Foy, Carol J Raport
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43332 (2012)
Chemokines play a key role in leukocyte recruitment during inflammation and are implicated in the pathogenesis of a number of autoimmune diseases. As such, inhibiting chemokine signaling has been of keen interest for the development of therapeutic ag
Externí odkaz:
https://doaj.org/article/dc762b06602041d28f80fcd50dabb157
Autor:
David L. Bienvenue, Robert Jedrzejczak, Tahirah K. Heath, Anna Starus, Cory T. Reidl, Andrzej Joachimiak, Boguslaw Nocek, Daniel P. Becker, Jerzy Osipiuk, Richard C. Holz
Publikováno v:
Biochemistry. 57:574-584
The X-ray crystal structure of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae (HiDapE) bound by the products of hydrolysis, succinic acid and l,l-DAP, was determined at 1.95 Å. Surprisingly, the structu
Autor:
Andrzej Joachimiak, Danuta Gillner, David L. Bienvenue, Vincentos Zachary, Boguslaw Nocek, Brian Bennett, Richard C. Holz
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 14:1-10
The catalytic and structural properties of the H67A and H349A dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae were investigated. On the basis of sequence alignment with the carboxypeptidase from Pseudo
Autor:
Brian Bennett, Sabina Swierczek, Ryan S. Davis, Lakshman Rajagopal, Danuta M. Gilner, David L. Bienvenue, Richard C. Holz
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 11:206-216
Glutamate-134 (E134) is proposed to act as the general acid/base during the hydrolysis reaction catalyzed by the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae. To date, no direct evidence has been re
Autor:
David L. Bienvenue, Carin C. Stamper, Gregory A. Petsko, Richard C. Holz, Brian Bennett, Dagmar Ringe
Publikováno v:
Biochemistry. 43:9620-9628
Binding of the competitive, slow-binding inhibitor bestatin ([(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoy]-leucine) to the aminopeptidase from Aeromonas proteolytica (AAP) was examined by both spectroscopic and crystallographic methods. Electronic abso
Autor:
Gregory A. Petsko, David L. Bienvenue, Krzysztof P. Bzymek, William Desmarais, Dagmar Ringe, Richard C. Holz
Publikováno v:
Structure. 10:1063-1072
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution c
Publikováno v:
Biochemistry. 41:3712-3719
A series of L-leucine aniline analogues were synthesized that contained either a carbonyl or thiocarbonyl as a part of the amide bond. Additionally, the para-position on the phenyl ring of several substrates was altered with various electron-withdraw
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 7:129-135
The aminopeptidase from Aeromonasproteolytica (AAP) can catalyze the hydrolysis of L-leucine ethyl ester (L-Leu-OEt) with a rate of 96±5 s–1 and a Km of 700 µM. The observed turnover number for L-Leu-OEt hydrolysis by AAP is similar to that obser
Autor:
Brian Bennett, Kristi M. Huntington, Yaoming Wei, David L. Bienvenue, Richard C. Holz, Dehua Pei
Publikováno v:
Biochemistry. 38:15587-15596
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 (K(I)) of thes
Autor:
David L. Bienvenue, Dagmar Ringe, Krzysztof P. Bzymek, William Desmarais, Richard C. Holz, Gregory A. Petsko
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 11(4)
The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in the active site and catalyzes the degradation of peptides. Herein we report the crystal structures of AAP at 0.95-A resolution at neutral pH and at 1.24-A resolution at lo