title: Purification and properties of pyruvate kinase from Thermoplasma acidophilum.
abstract: Thermoplasma acidophilum is a thermoacidophilic archaebacterium occupying a paradoxical place in phylogenetic trees (phenotypically it is a thermoacidophile but phylogenetically it classifies with the methanogens). To better understand its phylogeny, the pyruvate kinase from this organism is being investigated as a molecular marker. The enzyme has been purified and has a native M(r) of 250,000. It consists of four, apparently identical subunits each of M(r) 60,000. No remarkable kinetic differences have been found between this thermophilic enzyme and its mesophilic counterparts other than its greater thermostability. Its amino acid composition has been determined and some partial sequencing has been done.
authors.affiliation: Department of Biochemistry, University of Edinburgh, UK.
authors.forename: S
authors.initials: S
authors.lastname: Potter
authors.forename: L A
authors.initials: LA
authors.lastname: Fothergill-Gilmore
mesh_terms: D000595:Amino Acid Sequence; D000828:Animal Population Groups / Q000235:genetics; D000818:Animals; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010944:Plants / Q000235:genetics; D011770:Pyruvate Kinase / Q000302:isolation & purification* / Q000378:metabolism; D017385:Sequence Homology; D013045:Species Specificity; D013822:Thermoplasma / Q000201:enzymology* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D011770:Pyruvate Kinase