1.3.99.4	evolution	3-oxosteroid DELTA1-dehydrogenases are found in a large variety of microorganisms, especially in bacteria belonging to the phylum Actinobacteria	763443	
1.3.99.4	evolution	the genome of Rhodocccus ruber Chol-4 contains three genes that encode for 3-ketosteroid DELTA1-dehydrogenases: KstD1, KstD2 and KstD3. Their gene nucleotide sequences are similar to reciprocal homologues in other rhodococci. Physiological studies on strain Cho-4 and its kstD-deleted mutants demonstrate that the three dehydrogenases are involved in the catabolism of cholesterol at different degrees depending on catabolic intermediates. These KstDs are distinguished by their substrate profiles comprising C-19 and C-22 3-ketosteroids. Particularly, KstD3 has a preference for 5alpha-3-oxosteroids	763042	
1.3.99.4	malfunction	all ksdD-overexpressing strains (isozymes KsdD1-5) not only exhibit a faster initial conversion rate (increased by 22-102%) but also achieve a higher conversion ratio (increased by 15-66%) than that of the control strain during the conversion of 4-androstene-3,17-dione to 1,4-androstadiene-3,17-dione. Apparently, KsdD3 and KsdD2 have more effect on DELTA1-dehydrogenation	-, 763180	
1.3.99.4	malfunction	an enzyme-deficient mutant strain is unable to use cholesterol as a source of carbon and energy and has a limited ability to multiply. The mutant is unable to inhibit the NO and reactive oxygen species production induced through Toll-like receptor 2 signaling in infected resting macrophages, phenotpe, overview	-, 724670	
1.3.99.4	metabolism	oxosteroid-DELTA1-dehydrogenase (KstD) is a key enzyme in the metabolic pathway for chemical modifications of steroid hormones, overview of proposed pathway for phytosterols degradation in mycobacteria	-, 763441	
1.3.99.4	metabolism	the 3-ketosteroid-DELTA1-dehydrogenase is involved in steroid metabolism catalyzing the transformation of 4-androstene-3,17-dione to androst-1,4-diene-3,17-dione specifically	-, 725830	
1.3.99.4	additional information	enzyme residues Y125, Y365, and Y541 are essential to the function of KsdD, residues Y122, S138, and E140 contribute to the catalysis of KsdD, modelling of the enzyme-substrate bindung structure, overview	-, 763772	
1.3.99.4	additional information	homology-based structural analysis and structure modeling of KstD2 using the structure of SQ1-KstD1 Rhodococcus erythropolis SQ1 (PDB ID 4C3Y). Enzyme KstD1 and KstD2 belongs to clusters 1 and 2, respectively	-, 762659	
1.3.99.4	additional information	the key residues of isozyme KsdD5 with more versatility are revealed by structural modeling and site-directed mutagenesis. Enzyme residues Y528 and G532 act as an electrophile to promote labilization of the C2 hydrogen atoms of the 3-oxosteroid substrate. With the assistance of Y118, the general base Y355 captured the axial beta-hydrogen from the C2 atom as a proton, whereas FAD accepts the axial alpha-hydrogen from the C1 atom of the substrate as a hydride ion. Finally, a double bond between the C1 and C2 atoms is formed. Local models of the active site residues Y118, Y355, Y528, and G532, A255, R256, G258, G259, and L261, and F266 and R273 for KsdD5 with cofactor FAD	-, 763180	
1.3.99.4	additional information	three-dimensional structure of a 3-oxosteroid DELTA1-dehydrogenase and structure-function analysis, enzyme reaction mechanism analysis, overview	763443