The TM1072 gene from Thermotoga maritima codifies for a putative form of a rhamnulose-1-phosphate aldolase (Rha-1PA Tm). To investigate this enzyme further, its gene was cloned and expressed in Escherichia coli. The purified enzyme was activated by Co2+ as a divalent metal ion cofactor, instead of Zn2+ as its E. coli homologue, and exhibited a maximum of activity at 95 A degrees C. Furthermore, the enzyme displayed a high stability against extreme reaction conditions, retaining 90 % of its activity in the presence of 40 % of acetonitrile and showing a half-life greater than 3 h at 115 A degrees C. The kinetic parameters at room temperature (R/T) were also studied; the K (M) was calculated to be 3.6 A +/- 0.33 mM, while k (cat)/K (M) was found to be 0.7 x 10(3) s(-1) M-1. Given these characteristics, Rha-1PA Tm is an attractive enzyme for use as a biocatalyst for industrial applications, offering intriguing possibilities for practical biocatalysis.