EC Number   |
General Information |
Reference |
|---|
    1.14.15.30 | evolution |
KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices |
-, 744058 |
| 1.14.15.30 | malfunction |
deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione |
-, 744058 |
| 1.14.15.30 | malfunction |
deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione. A kshA disruption mutant of Mycobacterium smegmatis mc2 155 incubated with sitosterol accumulates 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione |
-, 744058 |
| 1.14.15.30 | malfunction |
deletion of the gene encoding the reductase component KshB of 3-ketosteroid 9alpha-hydroxylase in Rhodococcus equi strain USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione |
-, 745698 |
| 1.14.15.30 | malfunction |
DELTAkshA and DELTAkshB deletion mutants are unable to use cholesterol and 4-androstene-3,17-dione as primary carbon and energy sources and are unable to metabolize 5alpha-androstane-3,17-dione. The deletion of either of these genes leads to rapid death of the microorganism in murine infection models and in macrophages |
-, 716250 |
| 1.14.15.30 | malfunction |
gene deletion of kshA2 does not affect growth on 9alpha-hydroxy-4-androstene-3,17-dione, cholesterol, or cholic acid |
-, 717119 |
| 1.14.15.30 | malfunction |
Rhodococcus ruber strains devoid of any KshAB activity (DELTAkshB or DELTAkshA1,2,3 strains) are able to grow in cholesterol although 10times slower than the wild-type strain. This growth is due to the degradation of the side chain, a process that has been described to occur at different steps of the pathway being independent of the polycyclic ring opening. In the strain the side chain degradation process does not depend on any KshAB activity |
-, 745648 |
| 1.14.15.30 | metabolism |
3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid metabolism and can catalyze the transformation of 4-androstene-3,17-dione to 9alpha-hydroxy-4-androstene-3,17-dione |
-, 746503 |
| 1.14.15.30 | metabolism |
3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism |
-, 717735 |
| 1.14.15.30 | metabolism |
isoform KshA1 is a more versatile enzyme related to the cholic acid catabolism, although it also collaborates with KshA2 or KshA3 activities in the catabolism of steroids |
-, 745648 |
