publication . Other literature type . Article . 2003

Biochemical Properties and Regulated Gene Expression of the Superoxide Dismutase from the Facultatively Aerobic Hyperthermophile Pyrobaculum calidifontis

Taku Amo; Haruyuki Atomi; Tadayuki Imanaka;
Open Access English
  • Published: 01 Nov 2003
  • Publisher: American Society for Microbiology
Abstract
<jats:title>ABSTRACT</jats:title> <jats:p>Superoxide dismutase (SOD) was purified from a facultatively aerobic hyperthermophilic archaeon, <jats:italic>Pyrobaculum calidifontis</jats:italic> VA1. The purified native protein from aerobically grown cells exhibited 1,960 U of SOD activity/mg and contained 0.86 ± 0.04 manganese and &lt;0.01 iron atoms per subunit. The gene encoding SOD was cloned and expressed in <jats:italic>Escherichia coli</jats:italic>. Although the recombinant protein was soluble, little activity was observed due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn or Fe yielded a highly active prote...
Subjects
free text keywords: Enzymes and Proteins, Molecular Biology, Microbiology, Enzyme, chemistry.chemical_classification, chemistry, Biochemistry, Biology, Pyrobaculum, biology.organism_classification, Northern blot, Escherichia coli, medicine.disease_cause, medicine, Superoxide dismutase, biology.protein, Catalase, Hyperthermophile, Western blot, medicine.diagnostic_test
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publication . Other literature type . Article . 2003

Biochemical Properties and Regulated Gene Expression of the Superoxide Dismutase from the Facultatively Aerobic Hyperthermophile Pyrobaculum calidifontis

Taku Amo; Haruyuki Atomi; Tadayuki Imanaka;