Mechanistic Explanation of the Weak Carbonic Anhydrase's Esterase Activity.

نویسندگان

  • Paolo Piazzetta
  • Tiziana Marino
  • Nino Russo
چکیده

In order to elucidate the elementary mechanism of the promiscuous esterase activity of human carbonic anhydrase (h-CA), we present an accurate theoretical investigation on the hydrolysis of fully-acetylated d-glucose functionalized as sulfamate. This h-CA's inhibitor is of potential relevance in cancer therapy. The study has been performed within the framework of three-layer ONIOM (QM-high:QM'-medium:MM-low) hybrid approach. The computations revealed that the hydrolysis process is not energetically favored, in agreement with the observed weak carbonic anhydrase's esterase activity.

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

In vitro effect of ciprofibrate on human carbonic anhydrase II and glucose 6 phosphate dehydrogenase enzyme activities

Objective: Ciprofibrate (2-[4-(2,2-dichloro cyclopropyl) phenoxyl]-2-methyl propinoic acid) is a lipid-lowering drug used in the treatment of various metabolic diseases, especially hyperlipidemias. Human carbonic anhydrase II (hCA II) and glucose 6 phosphate dehydrogenase (G6PD) are crucial enzymes associated with many metabolic pathways. The aim of this study was to reveal the in vitro effect ...

متن کامل

Some drugs inhibit in vitro hydratase and esterase activities of human carbonic anhydrase-I and II.

In this study, we determined the in vitro inhibitory effects of ceftriaxone sodium, imipenem and ornidazole on hydratase and esterase activities of human erythrocyte carbonic anhydrase-I and II isozymes (CA I and II). Human erythrocyte CAI and II isozymes were purified by Sepharose-4B L-tyrosine affinity chromatography column with a yield of 30% and 40%, a specific activity of 920 and 8,000 EU/...

متن کامل

Monocarboxamidomethyl carbonic anhydrase purified by affinity chromatography.

A monocarboxamidomethyi derivative of human erythrocyte carbonic anhydrase B was purified by affinity chromatography. The modified enzyme possesses 3% of the COshydrating activity and 30% of the esterase activity of the native enzyme. The esterase activity is inhibited by the usual carbonic anhydrase inhibitors although the K; values are, in general, higher than for native enzyme. The pH depend...

متن کامل

Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and structural study.

This paper examines the functional mechanism of thioxolone, a compound recently identified as a weak inhibitor of human carbonic anhydrase II by Iyer et al. (2006) J. Biomol. Screening 11, 782-791 . Thioxolone lacks sulfonamide, sulfamate, or hydroxamate functional groups that are typically found in therapeutic carbonic anhydrase (CA) inhibitors, such as acetazolamide. Analytical chemistry and ...

متن کامل

Carbonic anhydrase (acetazolamide-sensitive esterase) activity in the blood, gill and kidney of the thermally acclimated rainbow trout, Salmo gairdneri.

1. Gill, kidney and blood levels of acetazolamide-sensitive esterase (carbonic anhydrase) activity were estimated at acclimation temperature and at a common temperature (25 degrees C) in rainbow trout acclimated to 2, 10 and 18 degrees C. Plasma levels of sodium, potassium and chloride were also examined for possible acclimatory variations. 2. Plasma sodium and chloride levels, and the sodium:c...

متن کامل

ذخیره در منابع من


  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:
  • Molecules

دوره 22 6  شماره 

صفحات  -

تاریخ انتشار 2017