Any feedback?
Information on EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
for references in articles please use BRENDA:EC1.1.1.292Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.292 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)IUBMB Comments
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 .
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
1,5-anhydro-D-fructose reductase, 1,5-anhydro-D-fructose reductase (ambiguous), AF reductase, AFR, AKR1E1, More, NADPH dependent 1,5-anhydro-D-fructose reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,5-anhydro-D-fructose reductase (ambiguous)
AF reductase
AFR
AKR1E1
NADPH dependent 1,5-anhydro-D-fructose reductase
additional information
additional information
the enzyme is a member of the aldo-keto reductase family 1
additional information
the enzyme is a member of the aldo-keto reductase family 1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
206138-19-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose + NADH + H+
1,5-anhydro-D-mannitol + NAD+
-
-
-
r
D-xylosone + NADPH + H+
D-lyxose + NADP+
17% of the activity with 1,5-anhydro-D-fructose
-
-
?
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
-
-
-
?
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
-
-
-
r
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
-
-
-
r
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
-
-
-
r
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
Streptococcus pneumoniae 110.58
-
-
-
r
1,5-anhydro-D-glucitol + NADP+
?
23% of the activity with 1,5-anhydro-D-mannitol
-
-
?
1,5-anhydro-D-glucitol + NADP+
?
23% of the activity with 1,5-anhydro-D-mannitol
-
-
?
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-fructose is the preferred substrate for the reductase reaction
-
-
r
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
-
-
-
r
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
1,5-anhydro-D-fructose is the preferred substrate for the reductase reaction
-
-
r
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
-
-
?
6-deoxy-D-glucosone + NADPH + H+
6-deoxy-D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-allosone + NADPH + H+
D-altrose + NADP+
10% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-allosone + NADPH + H+
D-altrose + NADP+
10% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-glucosone + NADPH + H+
D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
-
-
?
D-glucosone + NADPH + H+
D-mannose + NADP+
22% of the activity with 1,5-anhydro-D-fructose
-
-
?
additional information
?
-
D-glucose, D-fructose, glucuronic acid, DL-glyceraldehyde, formaldehyde, and acetone are poor substrates, substrate specificity of the recombinant enzyme, overview
-
-
?
additional information
?
-
D-glucose, D-fructose, glucuronic acid, DL-glyceraldehyde, formaldehyde, and acetone are poor substrates, substrate specificity of the recombinant enzyme, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
-
-
-
r
1,5-anhydro-D-fructose + NADPH + H+
1,5-anhydro-D-mannitol + NADP+
Streptococcus pneumoniae 110.58
-
-
-
r
1,5-anhydro-D-mannitol + NADP+
1,5-anhydro-D-fructose + NADPH
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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
NADPH
the N-terminal domain displays a Rossman fold and contains the cofactor binding site. The intact crystals contain the oxidized cofactor NADP+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
peptide FPPQSV is absolutely required for induction of the enzyme via AliB-like ORF 2, no activity without the peptide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
3.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G, cofactor: NADPH
6.4
1,5-Anhydro-D-fructose
pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
7.1
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
8.3
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme G206I, cofactor: NADPH
8.3
1,5-Anhydro-D-fructose
pH 6.5, native wild-type enzyme, cofactor: NADPH
8.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADPH
8.9
1,5-Anhydro-D-fructose
pH 8.0, mutant enzyme H180A, cofactor: NADPH
11.1
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADH
20.2
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
22.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme K94G, cofactor: NADPH
39
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
49
1,5-Anhydro-D-fructose
pH 7.5, mutant enzyme D176A, cofactor: NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
1,5-Anhydro-D-fructose
pH 7.5, mutant enzyme D176A, cofactor: NADPH
3.7
1,5-Anhydro-D-fructose
pH 8.0, mutant enzyme H180A, cofactor: NADPH
4.2
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme K94G, cofactor: NADPH
5.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
6.3
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
12.4
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADH
13.5
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
119
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G, cofactor: NADPH
145
1,5-Anhydro-D-fructose
pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
156
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme G206I, cofactor: NADPH
216
1,5-Anhydro-D-fructose
pH 6.5, native wild-type enzyme, cofactor: NADPH
369
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
405
1,5-Anhydro-D-fructose
pH 6.5, mutant enzyme A13G, cofactor: NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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
physiological function
Streptococcus pneumoniae 110.58
-
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
-
Show AA Sequence and Transmembrane Helices (2454 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A13G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.8fold higher than wild type value. Mutant enzyme shows activity with NADH as cofactor
G206I
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.4fold lower than wild type value
H180A
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 61.9fold lower than wild type value
K94G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 137fold lower than wild type value
S10G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.3fold higher than wild type value
S10G/A13G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 2fold higher than wild type value. Mutant enzyme shows activity with NADH as cofactor
S176A
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1001fold lower than wild type value
S33D/A13G
kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 84fold lower than wild type value. Mutant enzyme shows activity with NADH as cofactor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 17.6fold from Escherichia coli strain BL21 (DE3) by anion exchange and adsorption chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
gene afr, quantitative real-time RT-PCR enzyme expression analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Streptococcus pneumoniae 110.58
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuehn, A.; Yu, S.; Giffhorn, F.
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
Appl. Environ. Microbiol.
72
1248-1257
2006
Ensifer adhaerens (Q2I8V6), Ensifer adhaerens S-30.7.5 (Q2I8V6)
brenda
Dambe, T.R.; Kuehn, A.M.; Brossette, T.; Giffhorn, F.; Scheidig, A.J.
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
Biochemistry
45
10030-10042
2006
Ensifer adhaerens (Q2I8V6)
brenda
Sakuma, M.; Kubota, S.
Mouse AKR1E1 is an ortholog of pig liver NADPH dependent 1,5-anhydro-D-fructose reductase
Biosci. Biotechnol. Biochem.
72
872-876
2008
Mus musculus (Q9DCT1), Mus musculus C57/BL6J (Q9DCT1)
brenda
Schu, M.; Faust, A.; Stosik, B.; Kohring, G.W.; Giffhorn, F.; Scheidig, A.J.
The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation
Acta Crystallogr. Sect. F
69
844-849
2013
Sinorhizobium meliloti (Q92KZ3)
brenda
Nasher, F.; Foerster, S.; Yildirim, E.; Grandgirard, D.; Leib, S.; Heller, M.; Hathaway, L.
Foreign peptide triggers boost in pneumococcal metabolism and growth
BMC Microbiol.
18
23
2018
Streptococcus pneumoniae (A0A064C3N0), Streptococcus pneumoniae 110.58 (A0A064C3N0)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.292)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
