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

Description
  • 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
This object is in collection Permanent URL 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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dr26z890m
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