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PubMed1981

Protein synthesis in artemia salina. Eucaryotic elongation factor eEF-Ts is a transphosphorylase.

It is thought that eucaryotic elongation factor eEF-Ts catalyzes the replacement of GDP for GTP on eucaryotic elongation factor eEF-Tu. We have found that eEF-Ts displays a strong nucleoside diphosphate phosphotransferase activity. This transferase activity resides in a dimer molecule of a subunit molecular weight close to 30,000. The transfosforylating activity of eEF-Ts results in a stimulatory effect of ATP, GTP, UTP and CTP on protein synthesis provided that GDP is present. The specificity for guanine nucleotides in protein synthesis resides only in eEF-Tu.

Adenosine Triphosphate↗
PubMed1976

Resolution, specificity and transphosphorylase activity of calcifying cartilage alkaline phosphatases.

The phosphate releasing activity from calf scapula cartilage was resolved by DEAE-cellulose chromatography into two distinct phosphatase activities. The activity eluted first from the column (phosphatase I) was active towards a variety of phosphate esters and several linear oligo phosphates including sodium pyrophosphate, while the second phosphatase activity (phosphatase II) was active only towards simple phosphate esters. Phosphatase I acted towards oligo phosphates in a stepwise fashion hydrolyzing one phosphate at a time. Both phosphatase are sialoproteins and can transfer phosphate from any of their substrates into other than water phosphate acceptor molecules such as glycerol. By several criteria, it can be concluded that the two phosphatases are different enzyme entities.

Adenine Nucleotides↗