1.3.99.4	A255F	site-directed mutagenesis, inactive mutant	763180	
1.3.99.4	A255G	site-directed mutagenesis, inactive mutant	763180	
1.3.99.4	E140V	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	
1.3.99.4	F266A	site-directed mutagenesis, inactive mutant	-, 763180	
1.3.99.4	G258A	site-directed mutagenesis, inactive mutant	-, 763180	
1.3.99.4	G532A	site-directed mutagenesis, the mutant shows over 70% reduced activity compare to wild-type enzyme	763180	
1.3.99.4	L261A	site-directed mutagenesis, inactive mutant	763180	
1.3.99.4	additional information	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	
1.3.99.4	additional information	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	
1.3.99.4	additional information	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