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Content Apr 7, 2010 ... 3A9R. X-ray Structures of Bacillus pallidus D-Arabinose IsomeraseComplex with ... coi UP Sites UniProtKB Secstruc PDB Validation 3A9R.
Contentnoformatting Apr 7, 2010 ... 3A9R. X-ray Structures of Bacillus pallidus D-Arabinose IsomeraseComplex with ... coi UP Sites UniProtKB Secstruc PDB Validation 3A9R.
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Ogtitle RCSB PDB - 3A9R: X-ray Structures of Bacillus pallidus D-Arabinose IsomeraseComplex with (4R)-2-METHYLPENTANE-2,4-DIOL
Rating General
Ogdescription As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
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Content Database: PDB / ID: 3a9r. Structure ... Deposition, Nov 5, 2009, Deposition site: PDBJ / Processing site: PDBJ. Revision 1.0 ... CNS, 1.1, refinement. HKL-2000 ...
Contentnoformatting Database: PDB / ID: 3a9r. Structure ... Deposition, Nov 5, 2009, Deposition site: PDBJ / Processing site: PDBJ. Revision 1.0 ... CNS, 1.1, refinement. HKL-2000 ...
Title PDB-3a9r: X-ray Structures of Bacillus pallidus D-Arabinose ...
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Content The binding sites of Manganese atom in the structure of X-Ray Structures of Bacillus Pallidus D-Arabinose Isomerasecomplex With ... Click to enlarge, stereopicture of Manganese binding site 1 out of 6 in 3a9r. Click to ... Mn, N C: Ser398, 4.50.
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Name Manganese in the structure of X-Ray Structures of Bacillus Pallidus D-Arabinose Isomerasecomplex With (4R)-2-Methylpentane-2,4-Diol (pdb 3a9r)
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Contentnoformatting Superimposition of a active site and b substrate binding surface of RdFucI with EcFucI (PDB code: 1FUI), ApFucI (3A9R) and SpFucI (4C20). Close-up view of ...
Title Figure 7 | Enzymatic synthesis of l -fucose from l -fuculose using a ...
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Citationvolume 12
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Prismdoi doi:10.1186/s13068-019-1619-0
Citationtitle Enzymatic synthesis of l -fucose from l -fuculose using a fucose isomerase from Raoultella sp. and the biochemical and structural analyses of the enzyme
Journalid 13068
Citationarticletype Research
Dcsource Biotechnology for Biofuels 2019 12:1
Dcpublisher BioMed Central
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Citationabstract l-Fucose is a rare sugar with potential uses in the pharmaceutical, cosmetic, and food industries. The enzymatic approach using l-fucose isomerase, which interconverts l-fucose and l-fuculose, can be an efficient way of producing l-fucose for industrial applications. Here, we performed biochemical and structural analyses of l-fucose isomerase identified from a novel species of Raoultella (RdFucI). RdFucI exhibited higher enzymatic activity for l-fuculose than for l-fucose, and the rate for the reverse reaction of converting l-fuculose to l-fucose was higher than that for the forward reaction of converting l-fucose to l-fuculose. In the equilibrium mixture, a much higher proportion of l-fucose (~ ninefold) was achieved at 30 °C and pH 7, indicating that the enzyme-catalyzed reaction favors the formation of l-fucose from l-fuculose. When biochemical analysis was conducted using l-fuculose as the substrate, the optimal conditions for RdFucI activity were determined to be 40 °C and pH 10. However, the equ
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Dctitle Enzymatic synthesis of l -fucose from l -fuculose using a fucose isomerase from Raoultella sp. and the biochemical and structural analyses of the enzyme
Prismvolume 12
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Dccreator In Jung Kim
Dccopyright 2019 The Author(s)
Dcdescription l-Fucose is a rare sugar with potential uses in the pharmaceutical, cosmetic, and food industries. The enzymatic approach using l-fucose isomerase, which interconverts l-fucose and l-fuculose, can be an efficient way of producing l-fucose for industrial applications. Here, we performed biochemical and structural analyses of l-fucose isomerase identified from a novel species of Raoultella (RdFucI). RdFucI exhibited higher enzymatic activity for l-fuculose than for l-fucose, and the rate for the reverse reaction of converting l-fuculose to l-fucose was higher than that for the forward reaction of converting l-fucose to l-fuculose. In the equilibrium mixture, a much higher proportion of l-fucose (~ ninefold) was achieved at 30 °C and pH 7, indicating that the enzyme-catalyzed reaction favors the formation of l-fucose from l-fuculose. When biochemical analysis was conducted using l-fuculose as the substrate, the optimal conditions for RdFucI activity were determined to be 40 °C and pH 10. However, the equ
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Content Superimposition of a active site and b substrate binding surface of RdFucI with EcFucI (PDB code: 1FUI), ApFucI (3A9R) and SpFucI (4C20). Close-up view of ...
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Citationtitle Enzymatic synthesis of l -fucose from l -fuculose using a fucose isomerase from Raoultella sp. and the biochemical and structural analyses of the enzyme
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Citationabstract l-Fucose is a rare sugar with potential uses in the pharmaceutical, cosmetic, and food industries. The enzymatic approach using l-fucose isomerase, which interconverts l-fucose and l-fuculose, can be an efficient way of producing l-fucose for industrial applications. Here, we performed biochemical and structural analyses of l-fucose isomerase identified from a novel species of Raoultella (RdFucI). RdFucI exhibited higher enzymatic activity for l-fuculose than for l-fucose, and the rate for the reverse reaction of converting l-fuculose to l-fucose was higher than that for the forward reaction of converting l-fucose to l-fuculose. In the equilibrium mixture, a much higher proportion of l-fucose (~ ninefold) was achieved at 30 °C and pH 7, indicating that the enzyme-catalyzed reaction favors the formation of l-fucose from l-fuculose. When biochemical analysis was conducted using l-fuculose as the substrate, the optimal conditions for RdFucI activity were determined to be 40 °C and pH 10. However, the equ
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Dctitle Enzymatic synthesis of l -fucose from l -fuculose using a fucose isomerase from Raoultella sp. and the biochemical and structural analyses of the enzyme
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Dcdescription l-Fucose is a rare sugar with potential uses in the pharmaceutical, cosmetic, and food industries. The enzymatic approach using l-fucose isomerase, which interconverts l-fucose and l-fuculose, can be an efficient way of producing l-fucose for industrial applications. Here, we performed biochemical and structural analyses of l-fucose isomerase identified from a novel species of Raoultella (RdFucI). RdFucI exhibited higher enzymatic activity for l-fuculose than for l-fucose, and the rate for the reverse reaction of converting l-fuculose to l-fucose was higher than that for the forward reaction of converting l-fucose to l-fuculose. In the equilibrium mixture, a much higher proportion of l-fucose (~ ninefold) was achieved at 30 °C and pH 7, indicating that the enzyme-catalyzed reaction favors the formation of l-fucose from l-fuculose. When biochemical analysis was conducted using l-fuculose as the substrate, the optimal conditions for RdFucI activity were determined to be 40 °C and pH 10. However, the equ
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