Historic deactylases (HDACs) are members of an ancient enzyme family found in eukaryotes as well as in prokaryotes such as archae-bacteria and eubacteria. We here report a new histone deacetylase (Tea HDAC) that was cloned from the genomic library of Thermus caldophilus GK24 based on homology analysis with human historic deacetylase1 (HDAC1). The gene contains an open reading frame encoding 375 amino acids with a calculated molecular mass of 42,188 Da and the deduced amino acid sequence of Tea HDAC showed a 31% homology to human HDAC1. The Tea HDAC gene was over-expressed in Escherichia coli using a Glutathione-S transferase (GST) fusion vector (pGEX-4T-1) and the purified protein showed a deacetylase activity toward the fluorogenic substrate for HDAC. Moreover, the enzyme activity was inhibited by trichostatin A, a specific HDAC inhibitor, in a dose-dependent manner. Optimum temperature and pH of the enzyme was found to be approximately 70 degrees C and 7.0, respectively. In addition, zinc ion is required for catalytic activity of the enzyme. Together, these data demonstrate that Tca HDAC is a new histone deacetylase-like enzyme from T caldophilus GK24 and will be a useful tool for deciphering the role of HDAC in the prokaryote and development of new biochemical reactions. (c) 2007 Elsevier Inc. All rights reserved.