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Purification of a novel pyruvate kinase from a green alga
Author(s) -
Knowles Vicki L.,
Dennis David T.,
Plaxton William C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81511-x
Subject(s) - pyruvate kinase , biochemistry , protein subunit , pyruvate dehydrogenase complex , pkm2 , kinase , biology , enzyme , pyruvate dehydrogenase kinase , pyruvate dehydrogenase phosphatase , chloroplast , chlorophyta , chemistry , botany , algae , gene , glycolysis
A chloroplast pyruvate kinase has been purified to homogeneity from the green alga Selenastrum minutum . The subunit composition of the enzyme differs markedly from pyruvate kinases from other sources. Subunit and native M r s were 210 kDa and 235 kDa, respectively, indicating a monomeric structure. Immunological and peptide mapping analyses suggested structural homology to a bacterial, but not higher plant or mammalian pyruvate kinase.