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New pathway of utilization of ammonia nitrogen for the synthesis of amino acids through NADH dependent transaminases in Bombyx mori L.
Author(s) -
SESHACHALAM R.V.,
SUBRAMANYAM M. V. V.,
KRISHNAMOORTHY R. V.
Publication year - 1992
Publication title -
physiological entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 57
eISSN - 1365-3032
pISSN - 0307-6962
DOI - 10.1111/j.1365-3032.1992.tb01023.x
Subject(s) - bombyx mori , biology , transamination , voltinism , biochemistry , glutamine , asparagine , amino acid , fibroin , asparagine synthetase , transaminase , transferase , enzyme , glutamine synthetase , ammonia , larva , botany , silk , gene , computer science , operating system
. NADH dependent transamination was recorded for the first time in silkworm Bombyx mori (L.) eggs and in larval tissues. L‐Glutamine:2–oxoglutarate amino transferase (GOGAT) and L‐asparagine:2–oxoglutarate amino transferase (AOGAT) were determined in embryonic and also in larval tissues of multi‐and bivoltine races. The presence of these two enzymes coupled to glutamine synthetase indicated efficient utilization of metabolic ammonia hitherto unknown in higher organisms. It is proposed that these transfer enzymes help in building the free amino acid pool seen during the diapause and also in the fibroin synthesis in the last larval stadium.