Role of vitamin B12 and enzymes related to methylmalonyl-CoA mutase in a methanol-utilizing bacterium, Protaminobacter ruber.

نویسندگان

  • S Ueda
  • K Sato
  • S Shimizu
چکیده

A methanol-utilizing bacterium, Protaminobacter ruber, required cobalt ion or vitamin B12 as its growth factor, which could be replaced by succinate among various additions to the cobalt-deficient medium. The presence of adenosylcobalamin (adenosyl-B12)-dependent methylmalonyl-coenzyme A (CoA) mutase was demonstrated in the cell-free extracts of P. ruber. The specific activity of this mutase was not only fairly high in comparison with that reported with other organisms but also detected at a similar level throughout the cultivation period. The cell-free extracts of P. ruber grown on non-C1 compounds as a sole carbon and energy source also had methylmalonyl-CoA mutase activity. Furthermore, the extracts of this microorganism catalyzed the reactions from propionyl-CoA to succinyl-CoA and from alpha-ketoglutarate to alpha-hydroxyglutarate.

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

The presence of glutamate mutase in a methanol-utilizing bacterium, Protaminobacter ruber.

Cell-free extracts of a facultative methylotroph and strict aerobe, Protaminobacter ruber, could catalyze formation of beta-methylaspartate from glutamate. beta-Methylaspartate formed was further converted to mesaconate. From these results, it was found that the cells of P. ruber contained a sequential reaction system of glutamate mutase and beta-methylaspartase. The level of glutamate mutase a...

متن کامل

A protein having similarity with methylmalonyl-CoA mutase is required for the assimilation of methanol and ethanol by Methylobacterium extorquens AM1.

A 4.0 kb region of Methylobacterium extorquens AM1 DNA which complements three mutants unable to convert acetyl-CoA to glyoxylate (and therefore defective in the assimilation of methanol and ethanol) has been isolated and sequenced. It contains two ORFs and the 3'-end of a third one. The mutations in all three mutants mapped within the first ORF, which was designated meaA; it encodes a protein ...

متن کامل

Methylmalonyl-CoA mutase activity of leukocytes in variants and heterozygotes of methylmalonic acidemia.

An assay method for the methylmalonyl-CoA mutase of leukocytes obtained from 3 ml of blood was established. The enzyme activity which was measured with or without the in vitro addition of 5'-deoxyadenosylcobalamin was found to be of value for the diagnosis of two variants of methylmalonic acidemia (vitamin B12 responsive and unresponsive), and also for the detection of heterozygotes with the vi...

متن کامل

Uptake and physiological function of vitamin B12 in a photosynthetic unicellular coccolithophorid alga, Pleurochrysis carterae.

The photosynthetic coccolithophoid alga, Pleurochrysis (Hymenomonas) carterae, could take up and accumulate exogenous vitamin B12, most of which was converted into the coenzyme forms of vitamin B12. Two vitamin B12-dependent enzyme activities (methylmalonyl-CoA mutase, 2.6+/-0.4 nmol/min/mg protein and methionine synthase, 85.1+/-38.9 pmol/min/mg protein) could be found in a cell homogenate of ...

متن کامل

Effect of vitamin B12 deprivation on the in vivo levels of coenzyme A intermediates associated with propionate metabolism.

The in vivo coenzyme A intermediates involved in the metabolic pathway in which vitamin B,t serves as a coenzyme (conversion of methylmalonyl-CoA to succinyl-CoA) were measured in the livers of control and B12-deprived animals. Succinyl-CoA was assayed by the succinate thiokinase arsenolysis of succinyl-CoA coupled with 5’,5’-dithiobis(Znitrobenzoic acid) measurement of the liberated coenzyme A...

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:
  • Journal of nutritional science and vitaminology

دوره 24 5  شماره 

صفحات  -

تاریخ انتشار 1978