| dc.creator | AFFONSO, REGINA | |
| dc.creator | SAMPAIO, SUELEN de B. | |
| dc.creator | JANUARIO, FAGNER S. | |
| dc.creator | PEREIRA, LARISSA M. | |
| dc.creator | ARAG??O, DANIELLE S. | |
| dc.creator | CASARINI, DULCE E. | |
| dc.creator | ELIAS, CAROLINE C. | |
| dc.date | 2017 | |
| dc.date | 2020-05-18T18:52:28Z | |
| dc.date | 2020-05-18T18:52:28Z | |
| dc.date.accessioned | 2023-09-28T14:15:23Z | |
| dc.date.available | 2023-09-28T14:15:23Z | |
| dc.identifier | 2155-952X | |
| dc.identifier | http://repositorio.ipen.br/handle/123456789/31166 | |
| dc.identifier | 1 | |
| dc.identifier | 7 | |
| dc.identifier | 10.4172/2155-952X.C1.071 | |
| dc.identifier | Sem Percentil | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/9001389 | |
| dc.description | Angiotensin-converting enzyme I (ACE) is a membrane-bound that catalyzes the conversion of angiotensin I to the potent
vasopressor angiotensin II. ACE is a key part of the renin-angiotensin system, which regulates blood pressure and is widely
distributed throughout the body. There are two isoforms of human ACE, including the somatic ACE (sACE) present in somatic tissue
and the testicular ACE (tACE) present in male germinal cells. The sACE possesses two domains, N- C- domains, with catalytic sites
which exhibit 60% sequence identity. These domains differ in terms of chloride-ion activation profiles, rates of peptide hydrolysis
of angiotensin I, bradykinin, Goralatide, Luliberin, substance P, angiotensina, beta-amyloid peptide and sensitivities to various
inhibitors. A more detailed analysis shows that these regions are composed of HEMGH and EAIGD sequences that bind zinc ions to
facilitate catalytic activity (Fig. 1). Our question is: If the synthesis of catalytic sites with corrects structure and activity could be a good
model per si to study new drugs. The objective was to obtain the Ala361 a Gli468 and Ala959 to Ser1066 catalytic regions sACE in a structural
conformation that resembles its native form. The catalytic regions were obtained from bacterial system; the expression of this protein
in soluble form enables completion of the solubilization/purification steps without the need for refolding. The characterization of
Ala959 to Ser1066 region shows that this has an ??-helix and ??-strand structure, Fig. 1b, which zinc ion (essential for its activity) binds
to, and with enzymatic activity. Our conclusion is that the strategy used to obtain the Ala959 to Ser1066 region in the correct structural
conformation and with activity was successful. | |
| dc.format | 96-96 | |
| dc.relation | Journal of Biotechnology and Biomaterials | |
| dc.rights | openAccess | |
| dc.source | World Congress on Biotechnology and Biotech Industries Meet, 15th; International Conference on Enzymology and Molecular Biology, 2nd, March 20-21, 2017, Rome, Italy | |
| dc.subject | angiotensin | |
| dc.subject | enzyme inhibitors | |
| dc.subject | zinc ions | |
| dc.subject | bacteria | |
| dc.title | A new approach to obtain the catalytic sites region of human sACE with correct fold and activity | |
| dc.type | Resumos em peri??dicos | |
| dc.coverage | I | |
