Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling.

Pham, Viet-Laï.
Cadel, Marie-Sandrine.
Gouzy-Darmon, Cécile.
Hanquez, Chantal.
Beinfeld, Margery C.
Nicolas, Pierre.
Etchebest, Catherine.
Foulon, Thierry.
2007

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 more

Permanent URL
http://hdl.handle.net/10427/009963
Original publication
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.
ID: tufts:17304
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