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ß CARBOXYLATION ENZYMES IN MARINE PHYTOPLANKTON AND ISOLATION AND PURIFICATION OF PYRUVATE CARBOXYLASE FROM AMPHIDINIUM CARTERAE (DINOPHYCEAE) 1
Author(s) -
Appleby Geoffrey,
Colbeck Jill,
Holdsworth Eric S.,
Wadman Hugh
Publication year - 1980
Publication title -
journal of phycology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.85
H-Index - 127
eISSN - 1529-8817
pISSN - 0022-3646
DOI - 10.1111/j.1529-8817.1980.tb03033.x
Subject(s) - phaeodactylum tricornutum , biology , phosphoenolpyruvate carboxylase , pyruvate carboxylase , thalassiosira pseudonana , biochemistry , phosphoenolpyruvate carboxykinase , chlorella , carboxylation , botany , algae , enzyme , phytoplankton , ecology , catalysis , nutrient
The diatoms, Phaeodactylum tricornutum Bohlin, Cylindrotheca closterium var. californica (Meres.) Reim. & Lewin, Thalassiosira pseudonana Hasle & Heimdal and the prymnesiophyte Pavlova lutheri (Droop), Green, have been shown to contain phosphoenolpyruvate carboxykinase E.C.4.1.1.49. Another diatom Chaetoceros calcitrans (Paulsen) Takano, the chlorophyte Dunaliella tertiolecta Butcher, a rhodophyte Porphyridium cruentum Naegeli and the cyanophyte Anabaena cylindrica Lemmermann, all possessed phosphoenolpyruvate carboxylases E.G.4.1.1.31, which were stimulated by Mn ions and inhibited by malate and aspartate. Two dinoflagellates, Amphidinium carterae Hulbert and Gymnodinium sp., were shown to contain pyruvate carboxylase E.G.6.4.1.1., not previously reported in plants or marine algae. Pyruvate carboxylase was isolated and purified and found to contain biotin and it was inhibited by avidin and could be distinguished from the other two enzymes by complete inhibition by 5 mM Mn ions. The β carboxylating enzymes account for the anaplerotic formation of amino acids and intermediates of the tricarboxylic acid cycle formed during short‐term fixation of CO 2 .