BRENDA - Enzyme Database
show all sequences of 5.1.3.29

NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration

Ryu, K.S.; Kim, C.; Kim, I.; Yoo, S.; Choi, B.S.; Park, C.; J. Biol. Chem. 279, 25544-25548 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
alpha-L-fucopyranose
Escherichia coli
-
beta-L-fucopyranose
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AEN8
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-L-fucopyranose
-
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
alpha-L-fucopyranose
FucU binds to both alpha- and beta-fucopyranose and accelerates the conversion between them
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
additional information
FucU exhibits a pyranase activity for D-ribose. No activity with D-glucose, L-rhamnose and D-fucose
725359
Escherichia coli
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
FucU seems to require multimeric or dimeric structures for its enzymatic activity, because the N-terminally His-tagged FucU is an inactive monomer
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
alpha-L-fucopyranose
Escherichia coli
-
beta-L-fucopyranose
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-L-fucopyranose
-
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
alpha-L-fucopyranose
FucU binds to both alpha- and beta-fucopyranose and accelerates the conversion between them
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
additional information
FucU exhibits a pyranase activity for D-ribose. No activity with D-glucose, L-rhamnose and D-fucose
725359
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
FucU seems to require multimeric or dimeric structures for its enzymatic activity, because the N-terminally His-tagged FucU is an inactive monomer
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
27.9
-
alpha-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
65.1
-
beta-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
27.9
-
alpha-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
65.1
-
beta-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
Other publictions for EC 5.1.3.29
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
723846
Higgins
Structure of the fucose mutaro ...
Streptococcus pneumoniae
Acta Crystallogr. Sect. F
67
1524-1530
2011
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1
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4
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1
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1
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1
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1
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724666
Park
Male-like sexual behavior of f ...
Mus musculus
BMC Genet.
11
62
2010
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1
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1
1
-
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725706
Lee
Crystal structures and enzyme ...
Escherichia coli, Mus musculus
J. Mol. Biol.
391
178-191
2009
-
-
2
2
3
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2
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2
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2
1
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3
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2
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2
1
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725106
Park
Characterization and role of f ...
Homo sapiens, Mus musculus
Glycobiology
17
955-962
2007
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2
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2
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2
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2
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6
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3
1
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2
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2
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2
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6
-
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3
1
-
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-
-
-
-
-
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-
2
2
-
-
-
725359
Ryu
NMR application probes a novel ...
Escherichia coli
J. Biol. Chem.
279
25544-25548
2004
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1
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1
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1
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1
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1
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1
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1
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1
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