This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family . This enzyme differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose . The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones .
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
1,5-anhydro-D-mannitol:NADP+ oxidoreductase
This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family [2]. This enzyme differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose [1]. The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones [1].
D-glucose, D-fructose, glucuronic acid, DL-glyceraldehyde, formaldehyde, and acetone are poor substrates, substrate specificity of the recombinant enzyme, overview
D-glucose, D-fructose, glucuronic acid, DL-glyceraldehyde, formaldehyde, and acetone are poor substrates, substrate specificity of the recombinant enzyme, overview
wild-type enzyme and mutant enzymes S10G, S33D, K94G, D176A, H180A and G206I shows no activity with NADH. Mutant enzymes A13G, S10G/A13G and S33D/A13G are active with NADH
nonencapsulated Streptococcus pneumoniae bacteria are successful colonizers of the human nasopharynx and often possess genes aliB-like ORF 1 and 2 in place of capsule genes. AliB-like ORF 2 binds peptide FPPQSV, found in Prevotella species, resulting in enhanced colonization. 1,5-anhydro-D-fructose reductase is a metabolic enzyme of an alternative starch and glycogen degrading pathway found in many organisms, in both transcriptomic and proteomic data. The peptide increases expression of genes involved in release of host carbohydrates, carbohydrate uptake and carbohydrate metabolism. AliB-like ORF 2 confers an advantage in colonization by enhancing carbohydrate metabolism resulting in a boost in growth. This may explain the widespread presence of aliB-like ORF 2 in the nonencapsulated pneumococcal population in the human nasopharynx. Peptide FPPQSV is absolutely required for induction of enzyme 1,5-anhydro-D-fructose reductase (AFR) via AliB-like ORF 2, no activity without the peptide
nonencapsulated Streptococcus pneumoniae bacteria are successful colonizers of the human nasopharynx and often possess genes aliB-like ORF 1 and 2 in place of capsule genes. AliB-like ORF 2 binds peptide FPPQSV, found in Prevotella species, resulting in enhanced colonization. 1,5-anhydro-D-fructose reductase is a metabolic enzyme of an alternative starch and glycogen degrading pathway found in many organisms, in both transcriptomic and proteomic data. The peptide increases expression of genes involved in release of host carbohydrates, carbohydrate uptake and carbohydrate metabolism. AliB-like ORF 2 confers an advantage in colonization by enhancing carbohydrate metabolism resulting in a boost in growth. This may explain the widespread presence of aliB-like ORF 2 in the nonencapsulated pneumococcal population in the human nasopharynx. Peptide FPPQSV is absolutely required for induction of enzyme 1,5-anhydro-D-fructose reductase (AFR) via AliB-like ORF 2, no activity without the peptide
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, enzyme crystallized in complex with the cofactor NADP(H) and its structure is determined to 2.2 A resolution using selenomethionine single-wavelength anomalous dispersion
in complex with NADP(H), to 1.93 A resolution. The structure displays an empty substrate-binding, showing an open conformation of the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 may function as a molecular switch
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AKR1E1 gene, cloning from liver RNA, DNA and amino acid sequence determination, analysis, and comparison, expression in Escherichia coli strain BL21 (DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
peptide FPPQSV induces the expression of 1,5-anhydro-D-fructose (AF). The peptide is found in Prevotella species, resulting in enhanced colonization, proteomic analysis is performed by LC-MS/MS on wild-type strain 110.58 and mutant DELTAORF 2 in the presence and absence of AliB-like ORF 2 peptide ligand FPPQSV
peptide FPPQSV induces the expression of 1,5-anhydro-D-fructose (AF). The peptide is found in Prevotella species, resulting in enhanced colonization, proteomic analysis is performed by LC-MS/MS on wild-type strain 110.58 and mutant DELTAORF 2 in the presence and absence of AliB-like ORF 2 peptide ligand FPPQSV
peptide FPPQSV induces the expression of 1,5-anhydro-D-fructose (AF). The peptide is found in Prevotella species, resulting in enhanced colonization, proteomic analysis is performed by LC-MS/MS on wild-type strain 110.58 and mutant DELTAORF 2 in the presence and absence of AliB-like ORF 2 peptide ligand FPPQSV
Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis
Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis