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Evolutionary aspects of urea cycle enzyme genes
Author(s) -
Takiguchi Masaki,
Matsubasa Tadashi,
Amaya Yoshihiro,
Mori Masataka
Publication year - 1989
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950100506
Subject(s) - argininosuccinate lyase , urea cycle , enzyme , argininosuccinate synthase , arginase , biology , urea , biochemistry , gene , metabolic pathway , arginine , genetics , amino acid
The functions and expression pattern of urea cycle enzymes have undergone considerable changes during the course of evolution. Sequence analyses shows that urea cycle enzymes from mammals are homologous to microbial enzymes of the arginine‐metabolic pathway. Recently, an unexpected relationship was found between argininosuccinate lyase (EC 4.3.2.1), the fourth enzyme of the cycle, and δ‐crystallin, a lens structural protein of birds and reptiles.