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J. Biochem, 1988, Vol. 103, No. 4 622-628
© 1988 Japanese Biochemical Society

research-article

Thermostable Dipeptidase from Bacillus stearothermophilus: Its Purification, Characterization, and Comparison with Aminoacylase1

Hong-Yon Cho, Katsuyuki Tanizawa, Hidehiko Tanaka and Kenji Soda2

Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University Uji, Kyoto 611

2To whom correspondence should be addressed.

Dipeptidase (dipeptide hydrolase [EC 3.4.13.11 [EC] ]) has been purified to homogeneity and crystallized from the cell extract of Bacillus stearothermophilus IFO 12983. The enzyme has a molecular weight of about 86, 000, and is composed of two subunits identical in molecular weight (43,000). The enzyme contains 2 g atoms of zinc per mol of protein. A variety of dipeptides consisting of glycine or only L-amino acids serve as substrates of the enzyme; Km and Vmax values for L-valyl-L-alanine are 0.5 mM and 68.0 units/mg protein, respectively. The enzyme is significantly stable not only at high temperatures but also on treatment with protein denaturants such as urea and guanidine hydrochloride. The enzyme also catalyzes hydrolysis of several N-acylamino acids with Vmax values 3–30% of those for the hydrolysis of dipeptides. The thermostable dipeptidase shares various properties with bacterial aminoacylase [EC 3.5.1.14 [EC] ]: their subunit molecular weight, metal content and requirement, amino acid composition, and amino acid sequence in the N-terminal region are very similar.

1This study was supported in part by special coordination funds from the Science and Technology Agency of the Japanese Government.


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