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Results 1 - 10 of 33 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4A255F site-directed mutagenesis, inactive mutant 763180
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4A255G site-directed mutagenesis, inactive mutant 763180
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4E140V site-directed mutagenesis, no significant change in enzyme expression is caused by the mutation, the mutant shows reduced activity with 4-androstene-3,17-dione compared to wild-type enzyme 763772
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4F266A site-directed mutagenesis, inactive mutant -, 763180
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4G258A site-directed mutagenesis, inactive mutant -, 763180
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4G532A site-directed mutagenesis, the mutant shows over 70% reduced activity compare to wild-type enzyme 763180
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4L261A site-directed mutagenesis, inactive mutant 763180
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4more among the three KstD isozymes, KstD2 shows the highest enzymatic activity when expressed heterogeneously, and KstD1 performs poorly, especially in Escherichia coli. For isozyme KstD3, the KstD enzyme activities are hardly detected in either host, Escherichia coli or Bacillus subtilis -, 763441
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4more construction of a kstD1 deletion mutant. Among the three KstD isozymes, KstD2 shows the highest enzymatic activity when expressed heterogeneously, and KstD1 performs poorly, especially in Escherichia coli. For isozyme KstD3, the KstD enzyme activities are hardly detected in either host, Escherichia coli or Bacillus subtilis -, 763441
Show all pathways known for 1.3.99.4Display the word mapDisplay the reaction diagram Show all sequences 1.3.99.4more development of a synthetic 3-ketosteroid DELTA1-dehydrogenase (DELTA1-KstDA) for the generation of a catabolic pathway enabling cholesterol degradation in human cells. Coexpression with cholesterol-3-hydroxy-dehydrogenase (CholD) and 3-oxosteroid-9alpha-hydroxylase (Kst-9alphaH). CholD activity catalyzes the generation of a C-3 ketone, which is needed for DELTA1-KstD activity, which introduces a double bond between the C-1 and C-2 atoms of 3-oxosteroids. Cholesterol catabolism pathway in Actinomycetes, overview 763735
Results 1 - 10 of 33 > >>