2168-61-8

Usage

Uses

Used in Pharmaceutical Industry:
6'-Hydroxy Secophenol is used as a key intermediate in the synthesis of Cortistatins, a group of compounds with potent antiproliferative activity. These Cortistatins have been found to selectively inhibit the proliferation of human umbilical vein endothelial cells, making them a promising candidate for the development of novel therapeutic agents targeting angiogenesis-related diseases, such as cancer and age-related macular degeneration.
Used in Chemical Synthesis:
6'-Hydroxy Secophenol can be utilized as a building block in the synthesis of various complex organic molecules, including natural products and pharmaceuticals. Its unique structure and functional groups make it a valuable component in the development of new chemical entities with potential applications in various industries, such as pharmaceuticals, agrochemicals, and materials science.

Upstream product

• 2394-69-6 3-hydroxy-9,10-secoandrosta-1,3,5⁽¹⁰⁾-triene-9,17-dione 

Relevant academic research and scientific papers

A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism

Mycobacterium tuberculosis (Mtb) and Rhodococcus jostii RHA1 have similar cholesterol catabolic pathways. This pathway contributes to the pathogenicity of Mtb. The hsaAB cholesterol catabolic genes have been predicted to encode the oxygenase and reductase, respectively, of a flavin-dependent mono-oxygenase that hydroxylates 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (3-HSA) to a catechol. An hsaA deletion mutant of RHA1 did not grow on cholesterol but transformed the latter to 3-HSA and related metabolites in which each of the two keto groups was reduced: 3,9-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-17- one (3,9-DHSA) and 3,17-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9-one (3,17-DHSA). Purified 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione 4-hydroxylase (HsaAB) from Mtb had higher specificity for 3-HSA than for 3,17-DHSA (apparent kcat/Km = 1000 ± 100 M -1 s-1 versus 700 ± 100 M-1 s -1). However, 3,9-DHSA was a poorer substrate than 3-hydroxybiphenyl (apparent kcat/Km = 80 ± 40 M-1 s -1). In the presence of 3-HSA the Kmapp for O2 was 100 ± 10 μM. The crystal structure of HsaA to 2.5-A resolution revealed that the enzyme has the same fold, flavin-binding site, and catalytic residues as p-hydroxyphenyl acetate hydroxylase. However, HsaA has a much larger phenol-binding site, consistent with the enzyme's substrate specificity. In addition, a second crystal form of HsaA revealed that a C-terminal flap (Val367-Val394) could adopt two conformations differing by a rigid body rotation of 25° around Arg 366. This rotation appears to gate the likely flavin entrance to the active site. In docking studies with 3-HSA and flavin, the closed conformation provided a rationale for the enzyme's substrate specificity. Overall, the structural and functional data establish the physiological role of HsaAB and provide a basis to further investigate an important class of monooxygenases as well as the bacterial catabolism of steroids.