Enzymatic hydrolysis of 2,4-diketo acids.

نویسندگان

  • A MEISTER
  • J P GREENSTEIN
چکیده

In the course of studies on the desamidation of glutamine in rat liver extracts marked acceleration of this reaction was noted in the presence of 2,4-diketovaleric acid (acetopyruvic acid) .l Recent work indicates that pyruvic acid and certain other ar-keto acids increase the desamidation of glutamine in aqueous extracts of normal and neoplastic rat liver (l-3). Investigation of the mechanism of the acceleration of glutamine desamidation by 2,4-diketovaleric acid revealed that this effect was actually due to pyruvic acid formed by hydrolysis of the diketo acid and that 2,4-diketovaleric acid itself was apparently inactive in the glutamine system (4). This finding led to experiments on other 2,4-diketo acids. The present studies demonstrate the existence of a hitherto unrecognized enzymatic reaction occurring in extracts of liver and kidney, whereby a wide variety of 2,4-diketo acids (acylpyruvic acids) are hydrolyzed to yield pyruvic acid and the corresponding fatty acid.

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

Kinetic Modeling of Enzymatic Hydrolysis of Pretreated Sorghum Bicolor and Rice Husk

In this study, the hydrolysis of pretreated sorghum stem and rice husk was investigated at various initial enzyme concentrations and substrate loadings. The slowdown in enzymatic hydrolysis of lignocellulosic materials with conversion has often been attributed to decreasing the activity of enzyme. A kinetic model was developed and expressed mathematically based on enzyme deactivation for enzyma...

متن کامل

Human immunodeficiency virus type 1 (HIV-1) integrase: resistance to diketo acid integrase inhibitors impairs HIV-1 replication and integration and confers cross-resistance to L-chicoric acid.

The diketo acids are potent inhibitors of human immunodeficiency virus (HIV) integrase (IN). Mutations in IN, T66I, S153Y, and M154I, as well as T66I-S153Y and T66I-M154I double mutations, confer resistance to diketo acids (D. J. Hazuda et al., Science 287:646-650, 2000). The effects of these IN mutations on viral replication, enzymatic activity, and susceptibility to other HIV inhibitors are r...

متن کامل

Effects of Condition Enzymatic Hydrolysis on Degrees of Hydrolysis and Antioxidant Activity of Head Protein of Bighead (Aristichthys nobilis)

Background and Objectives: Enzymatic hydrolysis is an effective practical technology that recovers valuable proteins from far-less farmed fish without losing their nutritional characteristics. Enzymatic hydrolysis of protein sources such as aquatic animals is a type of protein recycling. In the present study, effects of temperature, time and concentration of papain enzyme on hydrolysis degree a...

متن کامل

Effects of Ultrasonic and High-Pressure Homogenization Pretreatment on the Enzymatic Hydrolysis and Antioxidant Activity of Yeast Protein Hydrolysate

Protein hydrolysate is highly regarded as a source of naturally occurring antioxidant peptides. The purpose of this study was to investigate the effect of Ultrasonic (Frequency, 20 KHz; Amplitude, 50%; Time, 30 min) and high-pressure homogenization (Power, 1500 bar; Rated flow, 10 dm/h) pretreatmenton the enzymatic hydrolysis and antioxidant properties of yeast protein hydrolysate obtained from...

متن کامل

Characterization of Yeast Protein Enzymatic Hydrolysis and Autolysis in Saccharomyces cerevisiae and Kluyveromyces marxianus

Protein recovery under sonication treatment and autolysis, also protein hydrolysis progress during enzymatic hydrolysis (using trypsin and chymotrypsin) and autolysis (using endogenous enzymes) were investigated in Saccharomyces cerevisiae and Kluyveromyces marxianus. Crude protein content of dried yeast cells were 53.22% and 45.6% for S.cerevisiae and K.marxianus, respectively. After 96 hrs of...

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 175 2  شماره 

صفحات  -

تاریخ انتشار 1948