title: Purification and characterization of the Clostridium josui porphobilinogen deaminase encoded by the hemC gene from a recombinant Escherichia coli.
abstract: The porphobilinogen deaminase encoded by the Clostridium josui hemC gene was purified from a recombinant Escherichia coli strain and its properties were characterized. The optimal temperature and pH of the purified enzyme were 65 degrees C and 7.0, respectively. This enzyme was quite thermostable: it retained 86% of the original activity after incubation at 70 degrees C for 1 h. The Km and Vmax values of the enzyme were 65 microM and 3.3 micromol/h/mg for porphobilinogen, respectively.
authors.affiliation: Faculty of Bioresources, Mie University, Tsu, Mie 514-8507, Japan.
authors.forename: E
authors.initials: E
authors.lastname: Fujino
authors.forename: T
authors.initials: T
authors.lastname: Fujino
authors.forename: S
authors.initials: S
authors.lastname: Karita
authors.forename: T
authors.initials: T
authors.lastname: Kimura
authors.forename: K
authors.initials: K
authors.lastname: Sakka
authors.forename: K
authors.initials: K
authors.lastname: Ohmiya