A 5′-nucleotidase from Neurospora crassa

Olson, Ann C.; Fraser, Murray

doi:10.1016/0005-2744(74)90159-4

Cited by 5 publications

(1 citation statement)

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“…5'Nase for dTMP and for dAMP of different origin was weakly inhibited by AdR but strongly by TdR and deoxyguanosine (10). In all kinds of examined material, 5'Nase was inhibited by ATP (3,7).…”

Section: Enzyme Activities In Mitochondria Of Normal and Regeneratingmentioning

confidence: 87%

Relationship between 5-Nucleotidase, Adenosine Deaminase, AMP Deaminase, ATP-(Mg^2+)-ase Activities and dTMP Kinase Activity in Rat Liver Mitochondria

Greger¹,

Fabianowska²

1979

Enzyme

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The activities of dTMP kinase (ATP-deoxythymidine monophosphate phosphotransferase, EC 2.7.4.9), 5'-nucleotidase (5'-ribonucleoside phosphohydrolase, EC 3.1.3.5), adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4), AMP deaminase (AMP aminohydrolase, EC 3.5.3.6) and ATP-(Mg^2+)-ase (ATP phosphohydrolase, EC 3.6.1.3) were assayed in mitochondria of normal and regenerating rat liver. In regenerating mitochondria, the dTMP kinase activity increased 20 times, 5'-nucleotidase (5'Nase) activity for dTMP diminished by 65% and its activity for other nucleoside monophosphates did not change; adenosine deaminase activity for adenosine (AR) increased by 40%, but for deoxyadenosine (AdR) decreased by 70%. AMP deaminase and ATP-(Mg^2+)-ase activities behaved similarly in mitochondria from regenerating liver, decreasing by 70 and 64% respectively. The changes of the amount of dTMP in mitochondria depend on enzyme activities which regulate the AdR concentration.

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Section: Enzyme Activities In Mitochondria Of Normal and Regeneratingmentioning

confidence: 87%