Carbamyl phosphate synthetase: studies on the mechanism of action.

نویسندگان

  • R L METZENBERG
  • M MARSHALL
  • P P COHEN
چکیده

The most noteworthy contrasts between the two reactions are the requirement for catalytic amounts of an appropriate derivative of glutamic acid in the case of the liver system, and the difference in stoichiometry with respect to nucleotides. As predicted from thermodynamics the bacterial system is freely reversible; the liver system is not. In this paper, evidence will be presented that the equation given above for the liver system represents the sum of two or more separable reactions, perhaps representing various aspects of the same enzyme.

برای دانلود رایگان 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

Biochemical Studies on Amphibian Metamorphosis

Thyroxine has been shown to accelerate the synthesis of carbamyl phosphate synthetase in the liver of Rana catesbeiana. Stimulation of carbamyl phosphate synthetase synthesis by thyroxine appears to be relatively specific because of the following observations: (1) succinoxidase activity decreased during the time that carbamyl phosphate synthetase increased; (2) liver catalase responded more slo...

متن کامل

The regulation of carbamyl phosphate synthetase (ammonia) in rat liver mitochondria. Effects of acetylglutamate concentration and ATP translocation.

1. Mitoplasts, unlike mitochondria, are readily permeable to acetylglutamate; by incubating mitoplasts with different external [acetylglutamate] a wide range of concentrations of this cofactor in the matrix can be obtained, which can be correlated directly with the velocity of carbamyl phosphate synthetase (ammonia). 2. The relationship between carbamyl phosphate synthetase (ammonia) activity a...

متن کامل

Rat liver glutamine synthetase. Preparation, properties, and mechanism of inhibition by carbamyl phosphate.

Glutamine synthetase, purified from rat liver, is homogeneous on acrylamide gel electrophoresis and on ultracentrifugation (~20,~) 15.0 S). The enzyme, which consists of eight subunits (subunit molecular weight, 44,000), resembles ovine brain glutamine synthetase in its physical properties, amino acid composition, and substrate specificity. Complete inhibition of the liver enzyme by methionine ...

متن کامل

Biochemical Studies on Amphibian Metamorphosis I. The effect of thyroxine on protein synthesis in the tadpole

Thyroxine has been shown to accelerate the synthesis of carbamyl phosphate synthetase in the liver of Rana catesbdana. Stimulation of carbamyl phosphate synthetase synthesis by thyroxine appears to be relatively specific because of the following observations: (I) succinoxidase activity decreased during the time that carbamyl phosphate synthetase increased; (2) liver catalase responded more slow...

متن کامل

Kinetic studies on rat liver carbamyl phosphate synthetase.

A partial purification of adult rat liver carbamyl phosphate synthetase is described. The mitochondrial enzyme has been purified to a specific activity of 23.3 pmoles of citrulline per hour per mg of protein. Kinetic studies reveal Michaelis constants for ammonium ion, bicarbonate, ATP, N-acetylglutamic acid, and magnesium similar to the reported values for frog liver carbamyl phosphate synthet...

متن کامل

Biochemical Studies on Amphibian Metamorphosis I. The effect of thyroxine on protein synthesis in the tadpole

Thyroxine has been shown to accelerate the synthesis of carbamyl phosphate synthetase in the liver of Rana catesbdana. Stimulation of carbamyl phosphate synthetase synthesis by thyroxine appears to be relatively specific because of the following observations: (I) succinoxidase activity decreased during the time that carbamyl phosphate synthetase increased; (2) liver catalase responded more slow...

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

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 233 6  شماره 

صفحات  -

تاریخ انتشار 1958