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Temperature‐induced selective death of the C‐domain within angiotensin‐converting enzyme molecule
Author(s) -
Voronov Sergei,
Zueva Natalia,
Orlov Victor,
Arutyunyan Alexander,
Kost Olga
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02888-0
Subject(s) - thermostability , chemistry , differential scanning calorimetry , enzyme , molecule , angiotensin converting enzyme , denaturation (fissile materials) , protein secondary structure , domain (mathematical analysis) , crystallography , folding (dsp implementation) , biophysics , active site , stereochemistry , biochemistry , biology , physics , thermodynamics , organic chemistry , mathematical analysis , mathematics , engineering , nuclear chemistry , blood pressure , electrical engineering , endocrinology
Somatic angiotensin‐converting enzyme (ACE) consists of two homologous domains, each domain bearing a catalytic site. Differential scanning calorimetry of the enzyme revealed two distinct thermal transitions with melting points at 55.3 and 70.5°C. which corresponded to denaturation of C‐ and N‐domains, respectively. Different heat stability of the domains underlies the methods of acquiring either single active N‐domain or active N‐domain with inactive C‐domain within parent somatic ACE. Selective denaturation of C‐domain supports the hypothesis of independent folding of the two domains within the ACE molecule. Modeling of ACE secondary structure revealed the difference in predicted structures of the two domains, which, in turn, allowed suggestion of the region 29–133 in amino acid sequence of the N‐part of the molecule as responsible for thermostability of the N‐domain.