Flavin changes accompanying adaptation of Zymobacterium oroticum to orotate.

نویسندگان

  • H KONDO
  • H C FRIEDMANN
  • B VENNESLAND
چکیده

The preceding paper describes the purification of the enzyme dihydroorotic dehydrogenase from the obligate anaerobe, Zgmobacterium oroticum (1) The enzyme is formed adaptively when the bacteria are grown on a complex medium containing orotate as a major energy source. Purification of dihydroorotic dehydrogenase led to the demonstration that the enzyme is a flavoprotein (1, 2). It therefore seemed possible that the adaptation to orotate might be accompanied by a change in the flavin content of the bacterial cells. The present paper describes measurements of the flavin content of dihydroorotic dehydrogenase, and of cells grown with either glucose or orotate as the energy source. Data will be presented to confirm the conclusion that the enzyme contains flavin mononucleotide and flavin adenine dinucleotide in approximately equal amounts, and to show that the bacteria grown on orotate contain considerably more F,MNr and F,4D than bacteria grown on glucose.

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

Crystalline dihydroorotic dehydrogenase.

Evidence has previously been presented that dihydroorotic dehydrogenase from Zymobacterium oroticum (1) is a flavoprotein (2). The present paper describes a procedure for crystallizing the enzyme as a globulin. Data are also presented to show that the protein crystals contain about one atom of iron per molecule of flavin, and that the flavin consists of both flavin mononucleotide and flavin ade...

متن کامل

Studies on dihydroorotate dehydrogenase by electron paramagnetic resonance spectroscopy. II. Electron paramagnetic resonance and optical spectra and titrations.

When dihydroorotate dehydrogenase, from Zymobacterium oroticum, was reduced by DPNH or dihydroorotate and examined by electron paramagnetic resonance spectrometry, a relatively intense free radical signal and the asymmetric signal at g = 1.94, found in many nonheme iron proteins, were observed within a few milliseconds. Both shape and saturation with microwave power of the free radical signals ...

متن کامل

Targeting Dihydro-orotate Dehydrogenase in C. difficile

Clostridium difficile (CD) is the leading hospital-associated infection in the UK with many strains possessing multiple-resistance to common antibiotics such as the fluoroquinolones, fusidic acid, erythromycin, clarithromycin and clindamycin (Cosello et al 2008). We have identified dihydroorotate dehydrogenase (DHODase) in C. difficile as a potential target for the development of pro-drug inhib...

متن کامل

Inhibition of synthesis of pyrimidine nucleotides by 2-hydroxy-3-(3,3-dichloroallyl)-1,4-naphthoquinone.

Dichboroablyblawsone [2-hydroxy-3-(3,3-dichboroallyb)-1 ,4naphthoquinone, NSC 126771 ] is of interest as an antiturnor agent. Like certain other naphthoquinones, it is known to be a respiratory poison as a result of interference with electron transport, but it has not been shown that this action is respon sible for its toxicity or antitiumor activity. Studies in cultured Li 210 cells showed tha...

متن کامل

Inhibition of dihydroorotate dehydrogenase activity by brequinar sodium.

The novel anticancer drug candidate brequinar sodium (DuP 785, NSC 368390, 6-fluoro-2-(2'-fluoro-1,1'-biphenyl-4-yl)-3-methyl-4-quinoline- carboxylic acid sodium salt) was shown previously to be an inhibitor of dihydroorotate dehydrogenase, the fourth enzyme of the de novo pyrimidine biosynthetic pathway. Brequinar sodium inhibits the activity of this enzyme isolated from mammalian sources only...

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 235  شماره 

صفحات  -

تاریخ انتشار 1960