Fatty acid synthesis by enzyme preparations of Clostridium kluyveri; a consideration of postulated 4-carbon intermediates in butyrate synthesis.

نویسندگان

  • E R STADTMAN
  • H A BARKER
چکیده

Reaction 1 was observed in cell-free enzyme preparations of C. kluyveri (21), but the participation of the remaining reactions is supported only by indirect evidence obtained from studies on other bacteria (2). Koepsell et al. (12) demonstrated the formation of butyryl phosphate from acetyl phosphate and butyrate by cell-free extracts of Clostridium butylicum; and Lipmann (13, 14) demonstrated the reversible transfer of phosphoryl groups between acetyl phosphate and the adenylic acid system by enzyme preparations of C. butylicum and La&bacillus delbrueckii, and further, postulated that the transfer of the phosphoryl group between acetyl phosphate and butyrate is mediated by adenosine pyrophosphate. In order to obtain a clearer insight into the mechanisms of fatty acid synthesis we have investigated the occurrence of Reactions 2, 3, and 4 and also several other reactions of acyl phosphates in enzyme preparations of C. lcluyveri.

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

Butyrate oxidation in the absence of inorganic phosphate by Clostridium kluyveri.

Preparations of soluble, cell-free enzymes of the bacterium Clostridium kluyveri, capable of carrying out both the synthesis and the oxidation of short chain fatty acids, have recently been described in a series of reports by Stadtman and Barker (16-21). The stability and activity of these enzyme preparations offer great advantages for the study in vitro of the mechanisms by which fatty acids a...

متن کامل

Fatty acid synthesis by enzyme preparations of Clostridium kluyveri; the aerobic oxidation of ethanol and butyrate with the formation of acetyl phosphate.

The anaerobic bacterium Clostdium kluyveti can catalyze the conversion of ethanol and acetate to butyrate and caproate (6). Tracer studies with growing cultures of this organism (2) have shown that this conversion involves an oxidation of ethanol to a a-carbon compound (“active” acetate) that is in approximate equilibrium with acetate. This activated a-carbon substance then condenses with ordin...

متن کامل

The production of fatty acids by a gram-negative coccus.

We have isolated from the rumen of the sheep an anaerobic Gram-negative coccus which ferments glucose, fructose, maltose, mannitol, sorbitol and DL-lactate with the production of hydrogen and carbon dioxide, acetate, propionate, n-butyrate, npentanoate and n-hexanoate (Elsden, Gilchrist, Lewis & Volcani, 1951). Since it is our intention to discuss the taxonomic position of this organism in a se...

متن کامل

Bacillus sp. PS35 Lipase-Immobilization on Styrene-Divinyl Benzene Resin and Application in Fatty Acid Methyl Ester Synthesis

Background: Lipase is an enzyme with immense application potential. Ester synthesis by lipase catalysis in organic media is an area of key industrial relevance. Enzymatic preparations with traits that cater to the needs of this function are hence being intensely researched. Objective: The objectives of the study were to immobilize the lipase from Bacillus sp. PS35 by cross-linking and adsorpti...

متن کامل

Acyl-bound Intermediates in Fatty Acid Synthesis.

This over-all equation is thought to consist of the repetition of a series of reactions, each series being initiated by the condensation of malonyl coenzyme A with an unsubstituted straight chain acyl compound to form ,&ketoacyl-S-enzyme (5, 8). A series is then presumably concluded by reactions in which the P-ketoacyl compound is reduced and dehydrated to form an acyl compound 2 carbon atoms l...

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:
  • The Journal of biological chemistry

دوره 184 2  شماره 

صفحات  -

تاریخ انتشار 1949