𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Characterisation of neprilysin (EC 3.4.24.11) S2′ subsite

✍ Scribed by Natalie Dion; Paul Cohen; Philippe Crine; Guy Boileau

Book ID
117107801
Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
498 KB
Volume
411
Category
Article
ISSN
0014-5793

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Studies on the structural feature of S'1
Studies on the structural feature of S'1 subsite of neprilysin (EC.3.4.24.11): Stereochemical requirement for the enzyme-inhibitor docking process
✍ Denis Danvy; Thierry Monteil; Jean-Christophe Plaquevent; Lucette Duhamel; Pierr 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 187 KB

The preferred conformation of thiorphan during the inhibitor-neprilysin docking process was investigated. A series of achiral inhibitors were tested. This study led to the design of a potent inhibitor, in which the ethylenic bond bears the aryl residue of P'I.

Selective Neurotensin-Derived Internally
Selective Neurotensin-Derived Internally Quenched Fluorogenic Substrates for Neurolysin (EC 3.4.24.16): Comparison with Thimet Oligopeptidase (EC 3.4.24.15) and Neprilysin (EC 3.4.24.11)
✍ Vitor Oliveira; Marcelo Campos; Jefferson P. Hemerly; Emer S. Ferro; Antonio C.M 📂 Article 📅 2001 🏛 Elsevier Science 🌐 English ⚖ 86 KB

Internally quenched fluorescent peptides derived from neurotensin (pELYENKPRRPYIL) sequence were synthesized and assayed as substrates for neurolysin (EC 3.4.24.16), thimet oligopeptidase (EC 3.4.24.15 or TOP), and neprilysin (EC 3.4.24.11 or NEP). Abz-LYENKPRRPYILQ-EDDnp (where EDDnp is N-(2,4-dini