INHIBITION OF CELLULAR PROLIFERATION USING AN INHIBITOR OF ASPARTATE TRANSCARBAMYLASE
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چکیده
منابع مشابه
Feedback inhibition of aspartate transcarbamylase in liver and in hepatoma.
Aspartate transcarbamylase was partially purified from rat liver, Morris hepatoma 5123-A or D, Hepatoma 7800, and Novikoff hepatoma and was shown to be inhibited by pyrimidine deoxyribonucleosides and deoxyribonucleotides. The pyrimidine ana logs, 5-bromo-2'-deoxyuridine, 5-bromouridine, 5-bromo-2'-deoxycytidine, 5-fluoro2'-deoxyuridine, 5-fluorouridine, 5-fluoro-2'-deoxycytidine, 5-iodo-2'-deo...
متن کاملAn intermediate complex in the dissociation of aspartate transcarbamylase.
The multisubunit enzyme aspartate transcarbamylase consists of six copies of two types of polypeptide chains, catalytic (C) and regulatory (R). A complex formed by the partial dissociation of this enzyme has been isolated. This species, which has the structure C(6)R(4), is a likely intermediate in the stepwise dissociation of aspartate transcarbamylase induced by mercurials. The formation of th...
متن کاملAspartate Transcarbamylase from Leishmania donovani
Leishmania donovani is a protozoal pathogen that belongs to the kinetoplastida order. Unlike in other eucaryotic systems, the first three enzymes of the de novo pyrimidine biosynthetic pathway are not components of a multifunctional protein system. The three enzyme activities in the crude extract were separated on a Sephacryl S-200 column. Aspartate carbamoyltransferase (EC 2.1.3.2) has been pu...
متن کاملProton Magnetic Relaxation of Aspartate Transcarbamylase
Nuclear magnetic relaxation methods were used to investigate the interaction of the inhibitor succinate with aspartate transcarbamylase from Escherichia coli. Over the pH range 7 to 9, the dissociation constant for succinate remains less than the inhibitor concentration used for most of this work (0.05 M). As a result, the enzyme predominantly exists in a single “gross” conformational state. Su...
متن کاملFunctionally important arginine residues of aspartate transcarbamylase.
The reaction of phenylglyoxal with aspartate transcarbamylase and its isolated catalytic subunit results in complete loss of enzymatic activity (Kantrowitz, E. R., and Lipscomb, W. N. (1976) J. Biol. Chem. 251, 2688-2695). If N-(phosphonacetyl)-L-aspartate is used to protect the active site, we find that phenylglyoxal causes destruction of the enzyme's susceptibility to activation by ATP and in...
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ژورنال
عنوان ژورنال: Pediatric Research
سال: 1974
ISSN: 0031-3998,1530-0447
DOI: 10.1203/00006450-197404000-00129