Open AccessOccurrence of the methylglyoxal bypass in halophilic Archaea
Author(s) -
Oren Aharon,
Gurevich Peter
Publication year - 1995
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.1574-6968.1995.tb07339.x
Subject(s) - methylglyoxal , haloferax volcanii , halophile , halobacterium , archaea , lactoylglutathione lyase , haloarchaea , biochemistry , enzyme , biology , salt (chemistry) , chemistry , bacteria , genetics , organic chemistry , gene
Eight species of halophilic Archaea were tested for the presence of the enzymes of the methylglyoxal bypass. Methylglyoxal synthase was found in extracts of all species tested, with the exception of Halobacterium salinarium and Halobacterium cutirubrum . The enzyme of Haloferax volcanii was most active at pH 7 in the absence of salt, and in the presence of 3 M NaCl or KCl activity was half of that without salt, and was inhibited by phosphate. Glyoxalase I was detected in all species tested. Optimal activity of H. volcanii glyoxalase I was found at pH 7 and 3 M KCl; in the absence of salt, activity was strongly reduced. Glutathione could be replaced by γ‐glutamylcysteine as the acceptor of the D‐lactoyl group. The work shows that the methylglyoxal bypass may be operative in representatives of the archaeal kingdom.