Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting
نویسندگان
چکیده
منابع مشابه
Staurosporine, a prolyl endopeptidase inhibitor.
anti-umnesic efTect on Alzheimer's rats.fi) In PCI2・ h cells staurosporine blocked NGF-induced neuriLe outgrowth at low doses. but at hLgher doses PCI2h cclls responded te staurospovine blr' rupid generation of neurites.4) The meehanisms of neurite outgrewth prompted by staurosporine might be difTl:Fent from that ofNGF. dB-cAMP, or infection witli a retrovirus carr},ing the v-src oncogene.4] It...
متن کاملSubstrate binding is the rate-limiting step in thromboxane synthase catalysis.
Thromboxane synthase (TXAS) is a "non-classical" cytochrome P450. Without any need for an external electron donor, or for a reductase or molecular oxygen, it uses prostaglandin H2 (PGH2) to catalyze either an isomerization reaction to form thromboxane A2 (TXA2) or a fragmentation reaction to form 12-l-hydroxy-5,8,10-heptadecatrienoic acid and malondialdehyde (MDA) at a ratio of 1:1:1 (TXA2:hept...
متن کاملA pH-dependent conformational change, rather than the chemical step, appears to be rate-limiting in the hammerhead ribozyme cleavage reaction.
We have investigated the chemical basis for a previously observed 7.8 A conformational change in the hammerhead ribozyme that positions the substrate for in-line attack. We have found that the conformational change can only be observed at or above pH 8.5 (in the presence of Co(2+)) and requires the presence of an ionizable 2'-OH at the cleavage site, and note that this observed apparent pK(a) o...
متن کاملQuestion Is phosphofructokinase the rate - limiting step of glycolysis ?
The quantitative aspects o f the regulation of glycolytic flux are still not well established. Even though convincing evidence that phosphofructokinase (PFK) participates in the regulation of the flux has been provided only for erythrocytes (albeit hexokinase seems to be more important in this respect) s, it is accepted that PFK is the main rate-controlling enzyme of glycolysis in different tis...
متن کاملEurystatins A and B, new prolyl endopeptidase inhibitors. II. Physico-chemical properties and structure determination.
The structures of eurystatins A and B, new prolyl endopeptidase inhibitors, have been elucidated by chemical degradation and spectral studies. They have in common a unique 13-membered cyclic peptide core composed of L-leucine, L-ornithine and (S)-3-amino-2-oxobutyric acid, and differ from each other in the alpha,beta-unsaturated fatty acid attached to the alpha-amino moiety of the ornithine.
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1992
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2830647