Rational Design of a β-Glycosidase with High Regiospecificity for Triterpenoid Tailoring
Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar‐hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such...
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Published in | Chembiochem : a European journal of chemical biology Vol. 16; no. 5; pp. 854 - 860 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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Weinheim
WILEY-VCH Verlag
23.03.2015
WILEY‐VCH Verlag |
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Abstract | Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar‐hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a β‐glycosidase with high regiospecificity for triterpenoids. A β‐glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 Å resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity.
Triterpenoids with desired glycosylation patterns are of great significance as potential therapeutics. A promiscuous β‐glycosidase was isolated and crystallized, and docking simulations led to rationally designed β‐glycosidases that produced specialty triterpenoids with high purity and regiospecificity. |
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AbstractList | Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar-hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a β-glycosidase with high regiospecificity for triterpenoids. A β-glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 Å resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity. Abstract Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar‐hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a β‐glycosidase with high regiospecificity for triterpenoids. A β‐glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 Å resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity. Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar‐hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a β‐glycosidase with high regiospecificity for triterpenoids. A β‐glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 Å resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity. Triterpenoids with desired glycosylation patterns are of great significance as potential therapeutics. A promiscuous β‐glycosidase was isolated and crystallized, and docking simulations led to rationally designed β‐glycosidases that produced specialty triterpenoids with high purity and regiospecificity. |
Author | Kyeong, Hyun-Ho Choi, Jung Min Kim, Song-Gun Park, Sang Jin Kim, Hak-Sung |
Author_xml | – sequence: 1 givenname: Sang Jin surname: Park fullname: Park, Sang Jin organization: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daehak-ro, Yuseong-gu, Daejeon, 305-701 (Korea) – sequence: 2 givenname: Jung Min surname: Choi fullname: Choi, Jung Min organization: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daehak-ro, Yuseong-gu, Daejeon, 305-701 (Korea) – sequence: 3 givenname: Hyun-Ho surname: Kyeong fullname: Kyeong, Hyun-Ho organization: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daehak-ro, Yuseong-gu, Daejeon, 305-701 (Korea) – sequence: 4 givenname: Song-Gun surname: Kim fullname: Kim, Song-Gun organization: Microbial Resource Center, Korea Research Institute of Bioscience & Biotechnology, Daejeon 305-806 (Korea) – sequence: 5 givenname: Hak-Sung surname: Kim fullname: Kim, Hak-Sung email: hskim76@kaist.ac.kr organization: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daehak-ro, Yuseong-gu, Daejeon, 305-701 (Korea) |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25703680$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_3390_foods12020397 crossref_primary_10_1016_j_jbiotec_2024_06_018 crossref_primary_10_1007_s00253_020_10455_9 crossref_primary_10_1016_j_fbio_2024_103829 |
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Keywords | rational design regiospecificity terpenoids binding mode glycosides |
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Snippet | Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types... Abstract Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and... |
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SubjectTerms | Actinomycetales - enzymology Actinomycetales - genetics beta-Glucosidase - chemistry beta-Glucosidase - genetics beta-Glucosidase - isolation & purification beta-Glucosidase - metabolism binding mode Biocatalysis glycosides Models, Molecular Molecular Conformation Mutation rational design regiospecificity Substrate Specificity terpenoids Triterpenes - chemistry Triterpenes - metabolism |
Title | Rational Design of a β-Glycosidase with High Regiospecificity for Triterpenoid Tailoring |
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