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IpdE1-IpdE2 is a heterotetrameric acyl coenzyme A dehydrogenase that is widely distributed in steroid-degrading bacteria by Gadbery, John; Round, James; Yuan, Tianao; Wipperman, Matthew F; Story, Keith Trizin; Crowe, Adam; Casabon, Israel; Liu, Jie; Yang, Xinxin; Eltis, Lindsay D.; Sampson, Nicole S is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Steroid-degrading bacteria, including (), utilize an architecturally distinct subfamily of acyl coenzyme A dehydrogenases (ACADs) for steroid catabolism. These ACADs are αβ heterotetramers that are usually encoded by adjacent like genes. In mycobacteria, and (formerly and ) occur in divergently transcribed operons associated with the catabolism of 3aα--4α(3'-propanoate)-7aβ-methylhexahydro-1,5-indanedione (HIP), a steroid metabolite. In , Δ and Δ mutants had similar phenotypes, showing impaired growth on cholesterol and accumulating 5-OH HIP in the culture supernatant. Bioinformatic analyses revealed that IpdE1 and IpdE2 share many of the features of the α- and β-subunits, respectively, of heterotetrameric ACADs that are encoded by adjacent genes in many steroid-degrading proteobacteria. When coproduced in a rhodococcal strain, IpdE1 and IpdE2 of formed a complex that catalyzed the dehydrogenation of 5OH-HIP coenzyme A (5OH-HIP-CoA) to 5OH-3aα--4α(3'-prop-1-enoate)-7aβ-methylhexa-hydro-1,5-indanedione coenzyme A (()5OH-HIPE-CoA). This corresponds to the initial step in the pathway that leads to degradation of steroid C and D rings via β-oxidation. Small-angle X-ray scattering revea

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Author
Gadbery, John; Round, James; Yuan, Tianao; Wipperman, Matthew F; Story, Keith Trizin; Crowe, Adam; Casabon, Israel; Liu, Jie; Yang, Xinxin; Eltis, Lindsay D.; Sampson, Nicole S
Publisher
American Chemical Society; American Chemical Society (ACS) (ISSN 0006-2960)
Published
2020
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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