Temperature‐induced selective death of the C‐domain within angiotensin‐converting enzyme molecule

FEBS Letters

Orlov, Victor²  Arutyunyan, Alexander²  Kost, Olga¹  Voronov, Sergei¹  Zueva, Natalia¹ 

[1]Chemistry Department, M.V. Lomonosov Moscow State University, Moscow 119992, Russia

[2]A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia

关键词: Peptidyl dipeptidase A;    Domain;    Enzyme stability;    Differential scanning calorimetry;    Circular dichroism;    Secondary protein structure;    ACE;    angiotensin-converting enzyme;    DSC;    differential scanning calorimetry;    SDS;    sodium dodecyl sulfate;    PMSF;    phenylmethylsulfonyl fluoride;    FA-Phe-Gly-Gly;    furanacryloyl-L-phenylalanyl-glycyl-glycine;    FA-Phe-Ala-Ala;    furanacryloyl-L-phenylalanyl-alanyl-alanine;    Hip-His-Leu;    N-benzoyl-glycyl-histidyl-leucine;    Cbz-Phe-His-Leu;    N-carbobenzoxy-phenylalanyl-histidyl-leucine;   

DOI  :  10.1016/S0014-5793(02)02888-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown