Journal article

Sequence comparisons of cytochrome P450 aromatases from Australian animals predict differences in enzymatic activity and/or efficiency

Anam Fatima, Jessica K Holien, Chandni Tiwari, Michael W Parker, Raymond J Rodgers, Lisandra L Martin

Biology of Reproduction | OXFORD UNIV PRESS INC | Published : 2020

Abstract

Aromatase (P450arom, CYP19A1) is the terminal enzyme in the synthesis of the steroid hormone family of estrogens. Not surprisingly, this enzyme has structural similarities between the limited number of species studied thus far. This study examined the structure of aromatases from four diverse Australian species including a marsupial (tammar wallaby; Macropus eugenii), monotreme (platypus; Ornithorhynchus anatinus), ratite (emu; Dromaius novaehollandiae) and lizard (bearded dragon; Pogona vitticeps). We successfully built homology models for each species, using the only crystallographically determined structure available, human aromatase. The amino acid sequences showed high amino acid sequen..

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Grants

Funding Acknowledgements

This research was supported by the National Health and Medical Research Council of Australia (NHMRC) and the Australian Research Council. This work was also supported by a capital grant from the Australian Cancer Research Foundation and infrastructure funding from the Victorian Government (Australia) Operational Infrastructure Support Scheme to St. Vincent's Institute of Medical Research. M.W.P. is a NHMRC Senior Principal Research Fellow, R.J.R. holds a Lloyd Cox Fellowship (University of Adelaide) and J.K.H. is a 5point Foundation Fellow.