Structural insight into a GH1 β-glucosidase from the oleaginous microalga,

Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-...
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Autor*in:	Dong, Sheng [verfasserIn] Liu, Ya-Jun [verfasserIn] Zhou, Haixia [verfasserIn] Xiao, Yan [verfasserIn] Xu, Jian [verfasserIn] Cui, Qiu [verfasserIn] Wang, Xinquan [verfasserIn] Feng, Yingang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	β-Glucosidase Laminaribiose Microalgae

Übergeordnetes Werk:	Enthalten in: International journal of biological macromolecules - New York, NY [u.a.] : Elsevier, 1979, 170, Seite 196-206
Übergeordnetes Werk:	volume:170 ; pages:196-206

DOI / URN:	10.1016/j.ijbiomac.2020.12.128

Katalog-ID:	ELV005441226

Internformat


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100	1		\|a Dong, Sheng \|e verfasserin \|4 aut
245	1	0	\|a Structural insight into a GH1 β-glucosidase from the oleaginous microalga,
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337			\|a Computermedien \|b c \|2 rdamedia
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520			\|a Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae.
650		4	\|a β-Glucosidase
650		4	\|a Laminaribiose
650		4	\|a Microalgae
700	1		\|a Liu, Ya-Jun \|e verfasserin \|4 aut
700	1		\|a Zhou, Haixia \|e verfasserin \|4 aut
700	1		\|a Xiao, Yan \|e verfasserin \|4 aut
700	1		\|a Xu, Jian \|e verfasserin \|4 aut
700	1		\|a Cui, Qiu \|e verfasserin \|4 aut
700	1		\|a Wang, Xinquan \|e verfasserin \|4 aut
700	1		\|a Feng, Yingang \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t International journal of biological macromolecules \|d New York, NY [u.a.] : Elsevier, 1979 \|g 170, Seite 196-206 \|h Online-Ressource \|w (DE-627)30089502X \|w (DE-600)1483284-7 \|w (DE-576)259270814 \|x 1879-0003 \|7 nnns
773	1	8	\|g volume:170 \|g pages:196-206
912			\|a GBV_USEFLAG_U
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912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_224
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
936	b	k	\|a 35.80 \|j Makromolekulare Chemie
936	b	k	\|a 58.30 \|j Biotechnologie
951			\|a AR
952			\|d 170 \|h 196-206

Indexfelder

author_variant	s d sd y j l yjl h z hz y x yx j x jx q c qc x w xw y f yf
matchkey_str	article:18790003:2020----::tutrlnihitahguoiaermho
hierarchy_sort_str	2020
bklnumber	35.80 58.30
publishDate	2020
allfields	10.1016/j.ijbiomac.2020.12.128 doi (DE-627)ELV005441226 (ELSEVIER)S0141-8130(20)35299-5 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Dong, Sheng verfasserin aut Structural insight into a GH1 β-glucosidase from the oleaginous microalga, 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae. β-Glucosidase Laminaribiose Microalgae Liu, Ya-Jun verfasserin aut Zhou, Haixia verfasserin aut Xiao, Yan verfasserin aut Xu, Jian verfasserin aut Cui, Qiu verfasserin aut Wang, Xinquan verfasserin aut Feng, Yingang verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 170, Seite 196-206 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:170 pages:196-206 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 170 196-206
spelling	10.1016/j.ijbiomac.2020.12.128 doi (DE-627)ELV005441226 (ELSEVIER)S0141-8130(20)35299-5 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Dong, Sheng verfasserin aut Structural insight into a GH1 β-glucosidase from the oleaginous microalga, 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae. β-Glucosidase Laminaribiose Microalgae Liu, Ya-Jun verfasserin aut Zhou, Haixia verfasserin aut Xiao, Yan verfasserin aut Xu, Jian verfasserin aut Cui, Qiu verfasserin aut Wang, Xinquan verfasserin aut Feng, Yingang verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 170, Seite 196-206 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:170 pages:196-206 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 170 196-206
allfields_unstemmed	10.1016/j.ijbiomac.2020.12.128 doi (DE-627)ELV005441226 (ELSEVIER)S0141-8130(20)35299-5 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Dong, Sheng verfasserin aut Structural insight into a GH1 β-glucosidase from the oleaginous microalga, 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae. β-Glucosidase Laminaribiose Microalgae Liu, Ya-Jun verfasserin aut Zhou, Haixia verfasserin aut Xiao, Yan verfasserin aut Xu, Jian verfasserin aut Cui, Qiu verfasserin aut Wang, Xinquan verfasserin aut Feng, Yingang verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 170, Seite 196-206 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:170 pages:196-206 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 170 196-206
allfieldsGer	10.1016/j.ijbiomac.2020.12.128 doi (DE-627)ELV005441226 (ELSEVIER)S0141-8130(20)35299-5 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Dong, Sheng verfasserin aut Structural insight into a GH1 β-glucosidase from the oleaginous microalga, 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae. β-Glucosidase Laminaribiose Microalgae Liu, Ya-Jun verfasserin aut Zhou, Haixia verfasserin aut Xiao, Yan verfasserin aut Xu, Jian verfasserin aut Cui, Qiu verfasserin aut Wang, Xinquan verfasserin aut Feng, Yingang verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 170, Seite 196-206 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:170 pages:196-206 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 170 196-206
allfieldsSound	10.1016/j.ijbiomac.2020.12.128 doi (DE-627)ELV005441226 (ELSEVIER)S0141-8130(20)35299-5 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Dong, Sheng verfasserin aut Structural insight into a GH1 β-glucosidase from the oleaginous microalga, 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae. β-Glucosidase Laminaribiose Microalgae Liu, Ya-Jun verfasserin aut Zhou, Haixia verfasserin aut Xiao, Yan verfasserin aut Xu, Jian verfasserin aut Cui, Qiu verfasserin aut Wang, Xinquan verfasserin aut Feng, Yingang verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 170, Seite 196-206 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:170 pages:196-206 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 170 196-206
language	English
source	Enthalten in International journal of biological macromolecules 170, Seite 196-206 volume:170 pages:196-206
sourceStr	Enthalten in International journal of biological macromolecules 170, Seite 196-206 volume:170 pages:196-206
format_phy_str_mv	Article
bklname	Makromolekulare Chemie Biotechnologie
institution	findex.gbv.de
topic_facet	β-Glucosidase Laminaribiose Microalgae
dewey-raw	540
isfreeaccess_bool	false
container_title	International journal of biological macromolecules
authorswithroles_txt_mv	Dong, Sheng @@aut@@ Liu, Ya-Jun @@aut@@ Zhou, Haixia @@aut@@ Xiao, Yan @@aut@@ Xu, Jian @@aut@@ Cui, Qiu @@aut@@ Wang, Xinquan @@aut@@ Feng, Yingang @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
hierarchy_top_id	30089502X
dewey-sort	3540
id	ELV005441226
language_de	englisch
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author	Dong, Sheng
spellingShingle	Dong, Sheng ddc 540 fid BIODIV bkl 35.80 bkl 58.30 misc β-Glucosidase misc Laminaribiose misc Microalgae Structural insight into a GH1 β-glucosidase from the oleaginous microalga,
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topic_title	540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Structural insight into a GH1 β-glucosidase from the oleaginous microalga β-Glucosidase Laminaribiose Microalgae
topic	ddc 540 fid BIODIV bkl 35.80 bkl 58.30 misc β-Glucosidase misc Laminaribiose misc Microalgae
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title	Structural insight into a GH1 β-glucosidase from the oleaginous microalga,
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title_full	Structural insight into a GH1 β-glucosidase from the oleaginous microalga
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doi_str_mv	10.1016/j.ijbiomac.2020.12.128
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title_sort	structural insight into a gh1 β-glucosidase from the oleaginous microalga
title_auth	Structural insight into a GH1 β-glucosidase from the oleaginous microalga,
abstract	Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae.
abstractGer	Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae.
abstract_unstemmed	Marine microalgae are promising sources of novel glycoside hydrolases (GHs), which have great value in biotechnical and industrial applications. Although many GH1 family β-glucosidases have been extensively studied, studies on β-glucosidases from microalgae are rare, and no structure of algal GH1 β-glucosidase has been reported. Here, we report the biochemical and structural study of a GH1 β-glucosidase BGLN1 from Nannochloropsis oceanica, an oleaginous microalga. Phylogenetic analysis of BGLN1, together with the known structures of GH1 β-glucosidases, has indicated that BGLN1 is branched at the root of the eukaryotic part of the phylogenetic tree. BGLN1 showed higher activity against laminaribiose compared to cello-oligosaccharides. Unlike most of the other GH1 β-glucosidases, BGLN1 is partially inhibited by metal ions. The crystal structure of BGLN1 revealed that BGLN1 adopts a typical (α/β)8-barrel fold with variations in loops and N-terminal regions. BGLN1 contains extra residues at the N-terminus, which are essential for maintaining protein stability. BGLN1 has a more acidic substrate-binding pocket than other β-glucosidases, and the variations beyond the conserved −1 site determine the substrate specificity. These results indicate that GH enzymes from microalgae may have unique structural and functional features, which will provide new insight into carbohydrate synthesis and metabolism in marine microalgae.
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title_short	Structural insight into a GH1 β-glucosidase from the oleaginous microalga,
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author2	Liu, Ya-Jun Zhou, Haixia Xiao, Yan Xu, Jian Cui, Qiu Wang, Xinquan Feng, Yingang
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doi_str	10.1016/j.ijbiomac.2020.12.128
up_date	2024-07-06T17:59:00.137Z
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Structural insight into a GH1 β-glucosidase from the oleaginous microalga,

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