| Description |
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Background: Aminopeptidase B (Ap-B; EC 3.4.11.6) catalyzes the cleavage
of basic residues at the N-terminus of peptides and processes glucagon into
miniglucagon. The enzyme exhibits, in vitro, a residual ability to hydrolyze
leukotriene A4 into the pro-inflammatory lipid mediator leukotriene B4. The potential
bi-functional nature of Ap-B ... read moreis supported by close structural relationships with LTA4
hydrolase (LTA4H ; EC 3.3.2.6). A structure-function analysis is necessary for the
detailed understanding of the enzymatic mechanisms of Ap-B and to design inhibitors,
which could be used to determine the complete in vivo functions of the
enzyme.
Keywords: aminopeptidase B, rat aminopeptidase B, His-tagged rat
aminopeptidase B, leukotriène A4 hydrolase, leukotriène A4, leukotriène B4, histidine
tag, Phenylmethylsulfonyl Fluoride, N-ethylmaleimide, aminopeptidase O,
thyrotropin-releasing hormone degrading enzyme, HEAT
domain:Hungtington-Elongation-A-subunit-TOR, ribonucleoprotein, Tricorn interacting
factor F3, aminopeptidase N from E. coli.
Springer Open.read less
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This object is in collection
| Citation |
- Pham, Viet-Laï, Marie-Sandrine Cadel, Cécile Gouzy-Darmon,
Chantal Hanquez, Margery C. Beinfeld, Pierre Nicolas, Catherine Etchebest, and
Thierry Foulon. "Aminopeptidase B, a glucagon-processing enzyme: site directed
mutagenesis of the Zn2+-binding motif and molecular modelling." BMC Biochemistry 8,
no. 1 (12, 2007): 1-20.
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