Novel inhibition of carbonic anhydrase isozymes I, II and III by carbamoyl phosphate.

نویسندگان

  • N D Carter
  • W R Chegwidden
  • D Hewett-Emmett
  • S Jeffery
  • A Shiels
  • R E Tashian
چکیده

Carbamoyl phosphate has been shown to inhibit carbonic anhydrase (CA) isozymes CA I, CA II and CA III. This physiologically important molecule is the most potent, naturally occurring inhibitor of carbonic anhydrase yet found. It is also unique, among carbonic anhydrase inhibitors discovered hitherto, in that it inhibits the 3 isozymes with equal effect, despite their strikingly different properties. The results imply the participation of carbonic anhydrase in the regulation of substrate availability for the urea cycle.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Testosterone-induced, sulfonamide-resistant carbonic anhydrase isozyme of rat liver is indistinguishable from skeletal muscle carbonic anhydrase III.

Three isozymes of carbonic anhydrase, CA I, CA II and CA III, have been characterized from the tissues of a variety of vertebrate species. CA I (low-activity, sulfonamide-sensitive form) has been found mainly in red cells but also occurs in other tissues (e.g., rumen epithelium, caecum, colonic mucosa, pituitary gland, ciliary body), CA II (high-activity, sulfonamide-sensitive form) is found in...

متن کامل

Carbonic Anhydrase Inhibitors. Part 461 Inhibition of Carbonic Anhydrase Isozymes I, II and IV With Trifluoromethylsulfonamide Derivatives and Their Zinc(II) and Copper(II) Complexes

Reaction of aromatic/heterocyclic sulfonamides containing a free amino group with triflic anhydride afforded compounds possessing trifluoromethanesulfonamido moieties in their molecule. The Zn(II) and Cu(II) complexes of these new sulfonamides were prepared and characterized by standard procedures (elemental analysis, spectroscopic, magnetic, thermogravimetric and conductimetric measurements). ...

متن کامل

Complexes With Biologically Active Ligands. Part 101 Inhibition of Carbonic Anhydrase Isozymes I and II With Metal Complexes of Imidazo[2,1−b ]-1,3,4-Thiadiazole-2-Sulfonamide

THE TITLE COMPOUND WAS PREPARED BY AN IMPROVED VARIANT OF THE LITERATURE PROCEDURE, AND METAL COMPLEXES CONTAINING ITS ANION AND THE FOLLOWING METAL IONS: Zn(II), Cd(II), Hg(II), Co(II), Ni(II), Cu(II), V(IV), Fe(III) and Ag(I) were synthesized and characterized by standard procedures (elemental analysis; IR, electronic, NMR and EPR spectroscopy; TG, magnetic and conductimetric measurements). T...

متن کامل

Inhibition of gluconeogenesis and urea synthesis in isolated rat hepatocytes by acetazolamide

Citrulline generation in isolated rat liver mitochondria is markedly inhibited by the carbonic anhydrase inhibitor acetazolamide (Dodgson et al., 1983). This finding suggests that hepatic mitochondrial-matrix carbonic anhydrase may exert an important controlling effect on ureogenesis by supplying bicarbonate for carbamoyl phosphate synthesis. Three different carbonic anhydrase isoenzymes have b...

متن کامل

Synthesis and carbonic anhydrase inhibitory properties of novel uracil derivatives.

Carbonic anhydrase (CA) inhibitors are valuable molecules based on several therapeutic applications, including antiglaucoma activity. In the present study, inhibition of two human cytosolic carbonic anhydrase isozymes I and II with some uracil derivatives (3-9) were investigated. Compounds 3-9 showed KI values in the range of 10.83-464 μM for hCA I and of 28.88-778.5 μM against hCA II, respecti...

متن کامل

ذخیره در منابع من

ذخیره در منابع من قبلا به منابع من ذحیره شده

{@ msg_add @}


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • FEBS letters

دوره 165 2  شماره 

صفحات  -

تاریخ انتشار 1984