Abstract:
:A Ser/Thr phosphatase gene cloned from Aspergillus oryzae, aoppt, revealed that the tetratricopeptide repeat (TPR) and catalytic domains of the full-length AoPPT are located at the N- and C-terminal regions, respectively, similar to those of human Ser/Thr phosphatase 5 (PP5) and yeast Ppt1. Four different regions of AoPPT, namely, a full-length polypeptide, the catalytic domain, the catalytic domain plus C-terminal 15 amino-acid residues and the TPR domain were expressed in Escherichia coli and their roles in dephosphorylation activity were examined, using p-nitrophenyl phosphate as the substrate. The full-length AoPPT showed the highest dephosphorylation activity while the catalytic domain had the lowest activity. The activity of the catalytic domain was not inhibited by the presence of the TPR domain and arachidonic acid did not increase the activity of the full-length enzyme. These findings suggest that the integrity of the entire enzyme would be necessary for its full activity to be expressed.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Feng B,Zhao CH,Tanaka S,Imanaka H,Imamura K,Nakanishi Kdoi
10.1016/j.ijbiomac.2007.03.005subject
Has Abstractpub_date
2007-08-01 00:00:00pages
281-5issue
3eissn
0141-8130issn
1879-0003pii
S0141-8130(07)00098-0journal_volume
41pub_type
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