The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity

Autor: Zenda Woodman, Mario R. W. Ehlers, Sylva L. U. Schwager, Pierre Redelinghuys, Edward D. Sturrock, Adriana K. Carmona

Publikováno v: Biochemical Journal. 389:739-744

sACE (somatic angiotensin-converting enzyme) consists of two homologous, N and C domains, whereas the testis isoenzyme [tACE (testis ACE)] consists of a single C domain. Both isoenzymes are shed from the cell surface by a sheddase activity, although

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f40047fd7459d8625403c7d9757aa07
https://doi.org/10.1042/bj20050187

Ace revisited: A new target for structure-based drug design

Autor: Edward D. Sturrock, K. Ravi Acharya, Mario R. W. Ehlers, James F. Riordan

Publikováno v: Nature Reviews. Drug Discovery

Key Points Angiotensin-converting enzyme (ACE) is a chloride-dependent metalloenzyme that catalyses the hydrolytic cleavage of dipeptides from the carboxyl terminus of many regulatory oligopeptides. ACE is central to the renin–angiotensin system th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::037ab45ffe3848af06b65ef4440c92da
http://europepmc.org/articles/PMC7097707

Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding

Autor: Susan PANG, Anthony J. CHUBB, Sylva L. U. SCHWAGER, Mario R. W. EHLERS, Edward D. STURROCK, Nigel M. HOOPER

Publikováno v: Biochemical Journal. 358:185-192

Angiotensin-converting enzyme (ACE) is one of a growing number of integral membrane proteins that is shed from the cell surface through proteolytic cleavage by a secretase. To investigate the requirements for ectodomain shedding, we replaced the glyc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dfcb56833835306bc170f15e75f043d0
https://doi.org/10.1042/bj3580185

Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites

Autor: Zenda Woodman, Edward D. Sturrock, Mario R. W. Ehlers, Wolf F. Brandt, Sylvester Y. Oppong, Sarah Cook, Sylva L. U. Schwager, Nigel M. Hooper

Publikováno v: Biochemical Journal. 347:711-718

The somatic and testis isoforms of angiotensin-converting enzyme (ACE) are both C-terminally anchored ectoproteins that are shed by an unidentified secretase. Although testis and somatic ACE both share the same stalk and membrane domains the latter w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b5fe38fc3bafd39d9874d1d41fdd68e4
https://doi.org/10.1042/bj3470711

Identification of Mycobacterium tuberculosis signal sequences that direct the export of a leaderless β-lactamase gene product in Escherichia coli

Autor: Fernanda M. P. R. da Silva Tatley, Hans Jürgen Hoffmann, Renate R. Scholle, Anthony J. Chubb, Zenda Woodman, Mario R. W. Ehlers

Publikováno v: Chubb, A J, Woodman, Z L, da Silva Tatley, F M, Hoffmann, H J, Scholle, R R & Ehlers, M R 1998, ' Identification of Mycobacterium tuberculosis signal sequences that direct the export of a leaderless beta-lactamase gene product in Escherichia coli ', Microbiology, vol. 144 ( Pt 6), pp. 1619-29 . https://doi.org/10.1099/00221287-144-6-1619

Proteins secreted by Mycobacterium tuberculosis may play a key role in virulence and may also constitute antigens that elicit the host immune response. However, the M. tuberculosis protein export machinery has not been characterized. A library of M.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fda85dbae73f331fbde198b1810bb93f
https://doi.org/10.1099/00221287-144-6-1619