EC Number   |
Protein Variants |
Reference |
|---|
    1.3.99.4 | Y119F |
almost complete loss of activity |
-, 742850 |
| 1.3.99.4 | Y318F |
almost complete loss of activity |
-, 742850 |
| 1.3.99.4 | Y487F |
almost complete loss of activity |
-, 742850 |
| 1.3.99.4 | more |
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 | more |
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 | more |
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 |
| 1.3.99.4 | more |
development of a synthetic 3-ketosteroid DELTA1-dehydrogenase (DELTA1-KstDR) 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. The downstream enzymes need to have equal or greater activity when compared to the enzymes acting upstream to allow the pathway to flow and to prevent the accumulation of toxic intermediates, kinetic study |
763735 |
| 1.3.99.4 | more |
enzyme from strain ST-095 only differs in residue V366 from strain JC-12 (S366). Mutation results in almost 3fold higher catalytic efficiency in strain JC-12 |
-, 743031 |
| 1.3.99.4 | more |
enzyme mutants are constructed based on in silico protein docking modeling using site-directed mutagenesis and exogenous expression |
-, 763772 |
| 1.3.99.4 | S325F |
mutant enzyme has no detectable KSTD enzyme activity |
-, 656722 |
