Search Results - "Bienvenue, D L"

Substrate Specificity, Metal Binding Properties, and Spectroscopic Characterization of the DapE-Encoded N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae by Bienvenue, David L, Gilner, Danuta M, Davis, Ryan S, Bennett, Brian, Holz, Richard C

“…The catalytic and structural properties of divalent metal ion cofactor binding sites in the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase…”
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Spectroscopic and X-ray Crystallographic Characterization of Bestatin Bound to the Aminopeptidase from Aeromonas (Vibrio) proteolytica by Stamper, Carin C, Bienvenue, David L, Bennett, Brian, Ringe, Dagmar, Petsko, Gregory A, Holz, Richard C

“…Binding of the competitive, slow-binding inhibitor bestatin ([(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoy]-leucine) to the aminopeptidase from Aeromonas…”
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Hydrolysis of Thionopeptides by the Aminopeptidase from Aeromonas proteolytica:  Insight into Substrate Binding by Bienvenue, David L, Gilner, Danuta, Holz, Richard C

“…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…”
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Slow-Binding Inhibition of the Aminopeptidase from Aeromonas proteolytica by Peptide Thiols: Synthesis and Spectroscopic Characterization by Huntington, Kristi M, Bienvenue, David L, Wei, Yaoming, Bennett, Brian, Holz, Richard C, Pei, Dehua

“…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…”
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Inhibition of the aminopeptidase from Aeromonas proteolytica by l-leucinethiol: kinetic and spectroscopic characterization of a slow, tight-binding inhibitor–enzyme complex by Bienvenue, David L, Bennett, Brian, Holz, Richard C

“…The peptide inhibitor l-leucinethiol (LeuSH) was found to be a potent, slow-binding inhibitor of the aminopeptidase from Aeromonas proteolytica (AAP). The…”
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The 1.20 AA Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition by Desmarais, W T, Bienvenue, D L, Bzymek, K P, Holz, R C, Petsko, G A, Ringe, D

“…The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully…”
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The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica by Desmarais, William, Bienvenue, David L, Bzymek, Krzysztof P, Petsko, Gregory A, Ringe, Dagmar, Holz, Richard C

“…The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in the active site and catalyzes the degradation of peptides. Herein we report the…”
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The dapE-encoded N-Succinyl-l,l-Diaminopimelic Acid Desuccinylase from Haemophilus influenzae Is a Dinuclear Metallohydrolase by COSPER, Nathaniel J., BIENVENUE, David L., SHOKES, Jacob E., GILNER, Danuta M., TSUKAMOTO, Takashi, SCOTT, Robert A., HOLZ, Richard C.

“…The Zn K-edge extended X-ray absorption fine structure (EXAFS) spectra, of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE) from…”
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The aminopeptidase from Aeromonas proteolytica can function as an esterase by Bienvenue, David L, Mathew, Rebecca S, Ringe, Dagmar, Holz, Richard C

“…The aminopeptidase from Aeromonas proteolytica (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…”
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