Computational based Structural, Functional and Phylogenetic Analyses Of 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate (DAHP) Synthase of Corynebacterium Spp
نویسندگان
چکیده
The pathway of aromatic amino acid biosynthesis was initiated by the enzyme DAHP synthase. In this branched biosynthetic pathway phenylalanine, tyrosine and tryptophan are produced. This enzyme was repressed and inhibited by three said end product of aromatic amino acids. The importance of this enzyme is microbial fermentation of aromatic amino acid production. The present study envisaged the in silico analysis of this protein (DAHP synthase). The structural, functional and phylogenetic studies of this protein of Corynebacteriumglutamicum have been determined and it was observed that the protein of interest is a thermostable, acidic protein having molecular weight ranging in between 38.67 to 52.32 kDa. KeywordsCorynebacterium; DAHP synthase; in silico study; aromatic amino acid __________________________________________________*****_________________________________________________
منابع مشابه
Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases.
3-Deoxy-D-manno-octulosonate 8-phosphate (KDOP) synthase and 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase catalyze similar phosphoenolpyruvate-utilizing reactions. The genome of Neisseria gonorrhoeae contains one gene encoding KDOP synthase and one gene encoding DAHP synthase. Of the two nonhomologous DAHP synthase families known, the N. gonorrhoeae protein belongs to the family ...
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