| Summary: | 碩士 === 國立陽明大學 === 生化暨分子生物研究所 === 102 === Nitrilases are ubiquitous enzymes existing in plants, animals, fungi and prokaryotes. First found in plants, nitrilase has been reported to play important roles by catalyzing indole-3-acetonitrile to indo-3-acetic acid (IAA), namely auxin. Nitrilases were mainly known and studied in plants before discovery of the mammalian family members whereas substrates were not known for mammalian Nit family members until lately. On the basis of global and structure-based sequence analysis, members of the nitrilase superfamily can now be classified into 13 branches, human NIT1 (36 kDa) was classified in branch 10 among C. elegans or D. melanogaster NitFhit. These nitrilases all possess a conserved Glu-Lys-Cys catalytic triad that could be responsible for nitrile and other non-peptide carbon-nitrogen catalysis. Its homolog human NIT2 has been identified as omega-amidase other than nitrile hydrolase a few years ago, thereby leaving the puzzles unanswered for human NIT1. In this study, the enzymatic properties of human NIT1 has been characterized.
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