Lysine- and lysine-plus-threonine-inhibitable aspartokinases in Bacillus brevis
作者： Michael J.M. Hitchcock , Brian Hodgson
DOI: 10.1016/0005-2744(76)90089-9
关键词: Psychological repression 、 Aspartate kinase 、 Biochemistry 、 Phosphotransferases 、 Isozyme 、 Biology 、 Molecular biology 、 Bacillus 、 Lysine 、 Enzyme 、 Threonine
摘要: Two aspartokinase (ATP:L-aspartate 4-phosphotrasferase, EC 2.7.2.4) enzyme activities have been identified and partially purified from Bacillus brevis. Aspartokinase I is subject to both inhibition repression by lysine, has a molecular weight in the region of 110 000. II lysine-stabilised enzyme, inhibited multivalently lysine plus theonine 95 This attern activity not described previously unusual that one end product (lysine) regulates two isoenzymes catalysing first reaction branced biosynthetic pathway. In absence changes more unstable non-inhibitable enzyme. Both enzymes are stabilised sulphydryl reducing agents similar affinities for ATP, aspartate lysine. However, there no evidence view they products common gene. Problem concerned with regulation species discussed.
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