A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]

Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
The American Society for Microbiology (ASM)
Published 2018
Publication Date:
2018-06-19
Publisher:
The American Society for Microbiology (ASM)
Print ISSN:
0099-2240
Electronic ISSN:
1098-5336
Topics:
Biology
Published by:
_version_ 1836398978734751744
autor Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
beschreibung In this study, we identified a P450 enzyme (STH10) and an oxidoreductase (POR) from Thanatephorus cucumeris NBRC 6298 by a combination of transcriptome sequencing and heterologous expression in Pichia pastoris . The biotransformation of 11-deoxycortisol was performed by using Pichia pastoris whole cells coexpressing sth10 and por , and the product analysis indicated that the STH10 enzyme possessed steroidal 19- and 11β-hydroxylase activities. This is a novel fungal P450 enzyme with 19-hydroxylase activity, which is different from the known steroidal aromatase cytochrome P450 19 (CYP19) and CYP11B families of enzymes. IMPORTANCE Hydroxylation is one of the most important reactions in steroid functionalization; in particular, C-19 hydroxylation produces a key intermediate for the synthesis of 19-nor-steroid drugs without a C-19 angular methyl group in three chemoenzymatic steps, in contrast to the current industrial process, which uses 10 chemical reactions. However, hydroxylation of the C-19 angular methyl group remains a very challenging task due to the high level of steric resistance to the C-19 methyl group between the A and B rings. The present report describes a novel fungal P450 enzyme with 19-hydroxylase activity. This opens a new venue for searching effective biocatalysts for the useful process of steroidal C-19 hydroxylation, although further studies for better understanding of the structural basis of the regioselectivity and substrate specificity of this fungal steroidal 19-hydroxylase are warranted to facilitate the engineering of this enzyme for industrial applications.
citation_standardnr 6286412
datenlieferant ipn_articles
feed_id 516
feed_publisher The American Society for Microbiology (ASM)
feed_publisher_url http://www.asm.org/
insertion_date 2018-06-19
journaleissn 1098-5336
journalissn 0099-2240
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher The American Society for Microbiology (ASM)
quelle Applied and Environmental Microbiology
relation http://aem.asm.org/cgi/content/short/84/13/e00503-18?rss=1
search_space articles
shingle_author_1 Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
shingle_author_2 Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
shingle_author_3 Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
shingle_author_4 Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
shingle_catch_all_1 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
In this study, we identified a P450 enzyme (STH10) and an oxidoreductase (POR) from Thanatephorus cucumeris NBRC 6298 by a combination of transcriptome sequencing and heterologous expression in Pichia pastoris . The biotransformation of 11-deoxycortisol was performed by using Pichia pastoris whole cells coexpressing sth10 and por , and the product analysis indicated that the STH10 enzyme possessed steroidal 19- and 11β-hydroxylase activities. This is a novel fungal P450 enzyme with 19-hydroxylase activity, which is different from the known steroidal aromatase cytochrome P450 19 (CYP19) and CYP11B families of enzymes. IMPORTANCE Hydroxylation is one of the most important reactions in steroid functionalization; in particular, C-19 hydroxylation produces a key intermediate for the synthesis of 19-nor-steroid drugs without a C-19 angular methyl group in three chemoenzymatic steps, in contrast to the current industrial process, which uses 10 chemical reactions. However, hydroxylation of the C-19 angular methyl group remains a very challenging task due to the high level of steric resistance to the C-19 methyl group between the A and B rings. The present report describes a novel fungal P450 enzyme with 19-hydroxylase activity. This opens a new venue for searching effective biocatalysts for the useful process of steroidal C-19 hydroxylation, although further studies for better understanding of the structural basis of the regioselectivity and substrate specificity of this fungal steroidal 19-hydroxylase are warranted to facilitate the engineering of this enzyme for industrial applications.
Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
The American Society for Microbiology (ASM)
0099-2240
00992240
1098-5336
10985336
shingle_catch_all_2 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
In this study, we identified a P450 enzyme (STH10) and an oxidoreductase (POR) from Thanatephorus cucumeris NBRC 6298 by a combination of transcriptome sequencing and heterologous expression in Pichia pastoris . The biotransformation of 11-deoxycortisol was performed by using Pichia pastoris whole cells coexpressing sth10 and por , and the product analysis indicated that the STH10 enzyme possessed steroidal 19- and 11β-hydroxylase activities. This is a novel fungal P450 enzyme with 19-hydroxylase activity, which is different from the known steroidal aromatase cytochrome P450 19 (CYP19) and CYP11B families of enzymes. IMPORTANCE Hydroxylation is one of the most important reactions in steroid functionalization; in particular, C-19 hydroxylation produces a key intermediate for the synthesis of 19-nor-steroid drugs without a C-19 angular methyl group in three chemoenzymatic steps, in contrast to the current industrial process, which uses 10 chemical reactions. However, hydroxylation of the C-19 angular methyl group remains a very challenging task due to the high level of steric resistance to the C-19 methyl group between the A and B rings. The present report describes a novel fungal P450 enzyme with 19-hydroxylase activity. This opens a new venue for searching effective biocatalysts for the useful process of steroidal C-19 hydroxylation, although further studies for better understanding of the structural basis of the regioselectivity and substrate specificity of this fungal steroidal 19-hydroxylase are warranted to facilitate the engineering of this enzyme for industrial applications.
Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
The American Society for Microbiology (ASM)
0099-2240
00992240
1098-5336
10985336
shingle_catch_all_3 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
In this study, we identified a P450 enzyme (STH10) and an oxidoreductase (POR) from Thanatephorus cucumeris NBRC 6298 by a combination of transcriptome sequencing and heterologous expression in Pichia pastoris . The biotransformation of 11-deoxycortisol was performed by using Pichia pastoris whole cells coexpressing sth10 and por , and the product analysis indicated that the STH10 enzyme possessed steroidal 19- and 11β-hydroxylase activities. This is a novel fungal P450 enzyme with 19-hydroxylase activity, which is different from the known steroidal aromatase cytochrome P450 19 (CYP19) and CYP11B families of enzymes. IMPORTANCE Hydroxylation is one of the most important reactions in steroid functionalization; in particular, C-19 hydroxylation produces a key intermediate for the synthesis of 19-nor-steroid drugs without a C-19 angular methyl group in three chemoenzymatic steps, in contrast to the current industrial process, which uses 10 chemical reactions. However, hydroxylation of the C-19 angular methyl group remains a very challenging task due to the high level of steric resistance to the C-19 methyl group between the A and B rings. The present report describes a novel fungal P450 enzyme with 19-hydroxylase activity. This opens a new venue for searching effective biocatalysts for the useful process of steroidal C-19 hydroxylation, although further studies for better understanding of the structural basis of the regioselectivity and substrate specificity of this fungal steroidal 19-hydroxylase are warranted to facilitate the engineering of this enzyme for industrial applications.
Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
The American Society for Microbiology (ASM)
0099-2240
00992240
1098-5336
10985336
shingle_catch_all_4 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
In this study, we identified a P450 enzyme (STH10) and an oxidoreductase (POR) from Thanatephorus cucumeris NBRC 6298 by a combination of transcriptome sequencing and heterologous expression in Pichia pastoris . The biotransformation of 11-deoxycortisol was performed by using Pichia pastoris whole cells coexpressing sth10 and por , and the product analysis indicated that the STH10 enzyme possessed steroidal 19- and 11β-hydroxylase activities. This is a novel fungal P450 enzyme with 19-hydroxylase activity, which is different from the known steroidal aromatase cytochrome P450 19 (CYP19) and CYP11B families of enzymes. IMPORTANCE Hydroxylation is one of the most important reactions in steroid functionalization; in particular, C-19 hydroxylation produces a key intermediate for the synthesis of 19-nor-steroid drugs without a C-19 angular methyl group in three chemoenzymatic steps, in contrast to the current industrial process, which uses 10 chemical reactions. However, hydroxylation of the C-19 angular methyl group remains a very challenging task due to the high level of steric resistance to the C-19 methyl group between the A and B rings. The present report describes a novel fungal P450 enzyme with 19-hydroxylase activity. This opens a new venue for searching effective biocatalysts for the useful process of steroidal C-19 hydroxylation, although further studies for better understanding of the structural basis of the regioselectivity and substrate specificity of this fungal steroidal 19-hydroxylase are warranted to facilitate the engineering of this enzyme for industrial applications.
Lu, W., Chen, X., Feng, J., Bao, Y.-J., Wang, Y., Wu, Q., Zhu, D.
The American Society for Microbiology (ASM)
0099-2240
00992240
1098-5336
10985336
shingle_title_1 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
shingle_title_2 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
shingle_title_3 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
shingle_title_4 A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
timestamp 2025-06-30T23:35:37.843Z
titel A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
titel_suche A Fungal P450 Enzyme from Thanatephorus cucumeris with Steroid Hydroxylation Capabilities [Biotechnology]
topic W
uid ipn_articles_6286412