Open AccessN ‐Hydroxides, aminotriazole, and cyanide activate ribulosebisphosphate carboxylase formation in Alcaligenes eutrophus
Author(s) -
Im DongSoo,
Friedrich* Cornelius G.
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb01444.x
Subject(s) - potassium cyanide , pyruvate carboxylase , biochemistry , carbon fixation , chemistry , cyanide , enzyme , alcaligenes , metabolism , rubisco , hydrogen cyanide , bacteria , biology , photosynthesis , organic chemistry , pseudomonas , genetics
Formation of the key enzyme of autotrophic carbon dioxide fixation ribulosebisphosphate carboxylase (RuBPCase) was studied in the facultatively lithoautotrophic hydrogen oxidizing bacterium Alcaligenes eutrophus . The enzyme was formed during heterotrophic growth on fructose. Addition of formamidoxime, acetaldoxime or hydroxyurea (10 mM) decreased the growth rate and increased RuBPCase‐specific activity 2‐ to 4‐fold. Aminotriazole (10 mM) and potassium cyanide (10 μM) stimulated RuBPCase formation 4‐ to 5‐fold. RuBPCase formation is derepressed in A. eutrophus under carbon starvation. This situation may be caused by these drugs besides their other reported interferences in the bacterial metabolism.