An enzyme, named GTP cyclohydorlase, that catalizes the hydrolytic removal of carbon No.S of GTP has been partially purified from extracts of Pseudomonas putida (IAM 1506). The enzyme exists in two molecuar weight forms : a high molecular weight form (150,000) and a low molecular weight from (40,000). The high molecular weight form has been purified 25-fold. Some of the properties of the enzyme are as follows : It functions optimally at pH8.0, and at $52^{circ}C$. The Km value for GTP is $20{mu}M$. Divalent cations $(Cd^{2+};and;Hg^{2+})$ 2+/) at a concentration of 5mM inhibit completely the enzyme activity. No metal ion including $Mg^{2+}$ is needed for the catalysis. The enzyme is heat labile ; its half at $57^{circ}C$ is 1.5 min. Of a number of nucleotides tested, only GDP was used to any extent as substrbte in place of GTP. One of the products of the enzyme is determined to be a dihydro-neopterin compound.