Taking Advantage of Promiscuity of Cold-Active Enzymes

Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the in...

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Main Authors:	Sondavid K. Nandanwar, Shweta Bharat Borkar, Jun Hyuck Lee, Hak Jun Kim
Format:	Article
Language:	English
Published:	MDPI AG 2020-11-01
Series:	Applied Sciences
Subjects:	cold-active enzyme catalytic efficiency broad substrate specificity substrate promiscuity psychrophile
Online Access:	https://www.mdpi.com/2076-3417/10/22/8128

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spelling	doaj-2938a36c7d4646ea9c7bc08fdd90cede2020-11-25T04:00:35ZengMDPI AGApplied Sciences2076-34172020-11-01108128812810.3390/app10228128Taking Advantage of Promiscuity of Cold-Active EnzymesSondavid K. Nandanwar0Shweta Bharat Borkar1Jun Hyuck Lee2Hak Jun Kim3Department of Marine Convergence Design Program, Pukyong National University, Busan 48513, KoreaDepartment of Chemistry, Pukyong National University, Busan 48513, KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 21990, KoreaDepartment of Chemistry, Pukyong National University, Busan 48513, KoreaCold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they could reduce the energy cost in the reaction, attenuate side-reactions, and simply be inactivated. In addition, the increased structural flexibility could result in broad substrate specificity for various non-native substrates, which is called substrate promiscuity. In this perspective, we deal with a less addressed aspect of cold-active enzymes, substrate promiscuity, which has enormous potential for semi-synthesis or enzymatic modification of fine chemicals and drugs. Further structural and directed-evolutional studies on substrate promiscuity of cold-active enzymes will provide a new workhorse in white biotechnology.https://www.mdpi.com/2076-3417/10/22/8128cold-active enzymecatalytic efficiencybroad substrate specificitysubstrate promiscuitypsychrophile
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Sondavid K. Nandanwar Shweta Bharat Borkar Jun Hyuck Lee Hak Jun Kim
spellingShingle	Sondavid K. Nandanwar Shweta Bharat Borkar Jun Hyuck Lee Hak Jun Kim Taking Advantage of Promiscuity of Cold-Active Enzymes Applied Sciences cold-active enzyme catalytic efficiency broad substrate specificity substrate promiscuity psychrophile
author_facet	Sondavid K. Nandanwar Shweta Bharat Borkar Jun Hyuck Lee Hak Jun Kim
author_sort	Sondavid K. Nandanwar
title	Taking Advantage of Promiscuity of Cold-Active Enzymes
title_short	Taking Advantage of Promiscuity of Cold-Active Enzymes
title_full	Taking Advantage of Promiscuity of Cold-Active Enzymes
title_fullStr	Taking Advantage of Promiscuity of Cold-Active Enzymes
title_full_unstemmed	Taking Advantage of Promiscuity of Cold-Active Enzymes
title_sort	taking advantage of promiscuity of cold-active enzymes
publisher	MDPI AG
series	Applied Sciences
issn	2076-3417
publishDate	2020-11-01
description	Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they could reduce the energy cost in the reaction, attenuate side-reactions, and simply be inactivated. In addition, the increased structural flexibility could result in broad substrate specificity for various non-native substrates, which is called substrate promiscuity. In this perspective, we deal with a less addressed aspect of cold-active enzymes, substrate promiscuity, which has enormous potential for semi-synthesis or enzymatic modification of fine chemicals and drugs. Further structural and directed-evolutional studies on substrate promiscuity of cold-active enzymes will provide a new workhorse in white biotechnology.
topic	cold-active enzyme catalytic efficiency broad substrate specificity substrate promiscuity psychrophile
url	https://www.mdpi.com/2076-3417/10/22/8128
work_keys_str_mv	AT sondavidknandanwar takingadvantageofpromiscuityofcoldactiveenzymes AT shwetabharatborkar takingadvantageofpromiscuityofcoldactiveenzymes AT junhyucklee takingadvantageofpromiscuityofcoldactiveenzymes AT hakjunkim takingadvantageofpromiscuityofcoldactiveenzymes
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Taking Advantage of Promiscuity of Cold-Active Enzymes

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