Characterization of Glu350 as a Critical Residue Involved in the N-Terminal Amine Binding Site of Aminopeptidase N (EC 3.4.11.2): Insights into Its Mechanism of Action-Reference-Cited by-同舟云学术

Characterization of Glu350 as a Critical Residue Involved in the N-Terminal Amine Binding Site of Aminopeptidase N (EC 3.4.11.2): Insights into Its Mechanism of Action

Published:1998-01-01 Issue:2 Volume:37 Page:686-692
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Luciani Nathalie¹,Marie-Claire Cynthia¹,Ruffet Emmanuel¹,Beaumont Ann¹,Roques Bernard P.¹,Fournié-Zaluski Marie-Claude¹

Affiliation:

1. Département de Pharmacochimie Moléculaire et Structurale, INSERM U266CNRS URA D 1500, UFR des Sciences Pharmaceutiques et Biologiques, 4, avenue de l'Observatoire, 75270 Paris Cedex 06, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi971705p

Reference48 articles.

1. Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N.

2. Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site

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