PMID- 22168 OWN - NLM STAT- MEDLINE DCOM- 19780127 LR - 20191027 IS - 0341-0382 (Print) IS - 0341-0382 (Linking) VI - 32 IP - 9-10 DP - 1977 Sep-Oct TI - On the mechanism of inactivation and ATP-dependent reactivation of rat liver tyrosine aminotransferase. PG - 777-80 AB - The mechanism of in vitro inactivation and ATP-dependent rapid reactivation of rat liver tyrosine aminotransferase by a membrane-bound system from rat liver and kidney cortex and the nucleotide specificity of this process was investigated using partially purified tyrosine amino-transferase as a substrate. Adenosine 5'-triphosphate (ATP) could be replaced by guanosine 5'-triphosphate (GTP), Whereas inosine 5'-triphosphate (ITP) was less effective. During reactivation [gamma-32P]ATP was incorporated into the enzyme and not excorporated by incubation of the labeled enzyme with excess non-radioative ATP. Inactivation of labeled tyrosine aminotransferase by a particulate fraction led to a decrease protein-bound radioactivity concomitant with an increase of [32P]orthophosphate. This points to a phosphorylation and dephosphorylation mechanism in the regulation of tyrosine aminotransferase activity. FAU - Hamm, H H AU - Hamm HH FAU - Seubert, W AU - Seubert W LA - eng PT - Journal Article PL - Germany TA - Z Naturforsch C Biosci JT - Zeitschrift fur Naturforschung. Section C, Biosciences JID - 7801143 RN - 5V5IOJ8338 (Pyridoxal Phosphate) RN - 8L70Q75FXE (Adenosine Triphosphate) RN - EC 2.6.1.5 (Tyrosine Transaminase) RN - I38ZP9992A (Magnesium) SB - IM MH - Adenosine Triphosphate/*pharmacology MH - Animals MH - Enzyme Activation/drug effects MH - Kinetics MH - Liver/*enzymology MH - Magnesium/pharmacology MH - Male MH - Pyridoxal Phosphate/pharmacology MH - Rats MH - Subcellular Fractions/enzymology MH - Tyrosine Transaminase/isolation & purification/*metabolism EDAT- 1977/09/01 00:00 MHDA- 1977/09/01 00:01 CRDT- 1977/09/01 00:00 PHST- 1977/09/01 00:00 [pubmed] PHST- 1977/09/01 00:01 [medline] PHST- 1977/09/01 00:00 [entrez] AID - 10.1515/znc-1977-9-1019 [doi] PST - ppublish SO - Z Naturforsch C Biosci. 1977 Sep-Oct;32(9-10):777-80. doi: 10.1515/znc-1977-9-1019.