Analysis of Glyceraldehyde 3-phosphate Dehydrogenase Gene in Lactarius Deliciosus Base on Bioinformatics

摘要

Glyceraldehyde 3-phosphate dehydrogenase is an enzyme that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In the present study, some characters of the amino acid sequence of GAPDH of L.deliciosus were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 20 kinds of amino acid; the theoretical pI of GAPDH was 7.08 and the theoretical molecular weight of GAPDH was 26165.9 Da; the total number of atoms was 3714. It was a stable protein. There were 7 glycosylation sites and it was a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD (P) binding fold. C-terminal domain is a mixed alpha/antiparallel beta fold.