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Purification and some properties of hydroxypyruvate isomerase of Bacillus fastidiosus

1980; Elsevier BV; Volume: 613; Issue: 2 Linguagem: Inglês

10.1016/0005-2744(80)90111-4

1878-1454

F. E. de Windt, Chris van der Drift,

Freezing and Crystallization Processes

Hydroxypyruvate isomerase of Bacillus fastidiosus is a novel enzyme (Braun, W. and Kaltwasser, H. (1979) Arch. Microbiol. 121, 129–134) which catalyzes the reversible conversion of tartronate semialdehyde into hydroxypyruvate. The enzyme was purified to homogeneity. The native molecule had a molecular weight of 265 000–280 000 and was composed of six subunits with a molecular weight of 45 000. The enzyme showed optimal activity at pH 6.6–7.4 and 57°C. Hydroxypyruvate isomerase is stable on heating for 10 min at 67°C. The enzyme appeared to be specific for tartronate semialdehyde and hydroxypyruvate and no cofactors were involved in the reaction. The equilibrium constant K=[tartronate semialdehyde][hydroxypyruvate] was found to be 2.5 at pH 7.1, and 30°C.