Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation

Abstract Cyanase catalyzes the bicarbonate-dependent degradation of cyanate to produce ammonia and carbon dioxide, and ammonia is a considerable alternative nitrogen source. Strikingly, the cyanase from the thermophilic fungus Thermomyces lanuginosus (Tl-Cyn) has the highest catalytic efficiency rep...

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Autores principales:	Bibhuti Ranjan, Philip H. Choi, Santhosh Pillai, Kugenthiren Permaul, Liang Tong, Suren Singh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/721db89b00704d46b1a1bc11ba2a2df8
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spelling	oai:doaj.org-article:721db89b00704d46b1a1bc11ba2a2df82021-12-02T14:12:43ZCrystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation10.1038/s41598-020-79489-32045-2322https://doaj.org/article/721db89b00704d46b1a1bc11ba2a2df82021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-79489-3https://doaj.org/toc/2045-2322Abstract Cyanase catalyzes the bicarbonate-dependent degradation of cyanate to produce ammonia and carbon dioxide, and ammonia is a considerable alternative nitrogen source. Strikingly, the cyanase from the thermophilic fungus Thermomyces lanuginosus (Tl-Cyn) has the highest catalytic efficiency reported among these enzymes. However, its molecular mechanism of action is not clearly understood, because currently there is no structural information available on fungal cyanases. Here we report the crystal structure of Tl-Cyn in complex with inhibitors malonate and formate at 2.2 Å resolution. The structure reveals extensive interactions at the subunit interfaces in a dimer, and a decamer is formed by a pentamer of these dimers. Our biochemical, kinetic and mutagenesis studies confirm the structural observations on the complex and provide further insights into its catalytic mechanism and inhibition. The structure has also aided the creation of a mutant enzyme with enhanced catalytic activity, and such enzymes may have the potential for biotechnological applications, including biotransformation and bioremediation. Moreover, other fungal cyanases with potentially high catalytic activity could also be predicted based on the Tl-Cyn structure, as the active site region among fungal cyanases are highly conserved.Bibhuti RanjanPhilip H. ChoiSanthosh PillaiKugenthiren PermaulLiang TongSuren SinghNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Bibhuti Ranjan Philip H. Choi Santhosh Pillai Kugenthiren Permaul Liang Tong Suren Singh Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
description	Abstract Cyanase catalyzes the bicarbonate-dependent degradation of cyanate to produce ammonia and carbon dioxide, and ammonia is a considerable alternative nitrogen source. Strikingly, the cyanase from the thermophilic fungus Thermomyces lanuginosus (Tl-Cyn) has the highest catalytic efficiency reported among these enzymes. However, its molecular mechanism of action is not clearly understood, because currently there is no structural information available on fungal cyanases. Here we report the crystal structure of Tl-Cyn in complex with inhibitors malonate and formate at 2.2 Å resolution. The structure reveals extensive interactions at the subunit interfaces in a dimer, and a decamer is formed by a pentamer of these dimers. Our biochemical, kinetic and mutagenesis studies confirm the structural observations on the complex and provide further insights into its catalytic mechanism and inhibition. The structure has also aided the creation of a mutant enzyme with enhanced catalytic activity, and such enzymes may have the potential for biotechnological applications, including biotransformation and bioremediation. Moreover, other fungal cyanases with potentially high catalytic activity could also be predicted based on the Tl-Cyn structure, as the active site region among fungal cyanases are highly conserved.
format	article
author	Bibhuti Ranjan Philip H. Choi Santhosh Pillai Kugenthiren Permaul Liang Tong Suren Singh
author_facet	Bibhuti Ranjan Philip H. Choi Santhosh Pillai Kugenthiren Permaul Liang Tong Suren Singh
author_sort	Bibhuti Ranjan
title	Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
title_short	Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
title_full	Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
title_fullStr	Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
title_full_unstemmed	Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
title_sort	crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/721db89b00704d46b1a1bc11ba2a2df8
work_keys_str_mv	AT bibhutiranjan crystalstructureofathermophilicfungalcyanaseanditsimplicationsonthecatalyticmechanismforbioremediation AT philiphchoi crystalstructureofathermophilicfungalcyanaseanditsimplicationsonthecatalyticmechanismforbioremediation AT santhoshpillai crystalstructureofathermophilicfungalcyanaseanditsimplicationsonthecatalyticmechanismforbioremediation AT kugenthirenpermaul crystalstructureofathermophilicfungalcyanaseanditsimplicationsonthecatalyticmechanismforbioremediation AT liangtong crystalstructureofathermophilicfungalcyanaseanditsimplicationsonthecatalyticmechanismforbioremediation AT surensingh crystalstructureofathermophilicfungalcyanaseanditsimplicationsonthecatalyticmechanismforbioremediation
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Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation

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