BRENDA - Enzyme Database

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)
EC Number
Commentary
Organism
5.1.3.29
-
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
5.4.99.62
H106A
the mutant enzyme retains one-third of the original pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does,
Escherichia coli
5.4.99.62
H20A
mutation completely abolishes the pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does,
Escherichia coli
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5.1.3.29
alpha-L-fucopyranose
Escherichia coli
-
beta-L-fucopyranose
-
-
r
5.1.3.32
alpha-L-rhamnopyranose
Escherichia coli
-
beta-L-rhamnopyranose
-
-
?
5.4.99.62
beta-D-ribopyranose
Escherichia coli
-
beta-D-ribofuranose
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.1.3.29
Escherichia coli
P0AEN8
-
-
5.1.3.32
Escherichia coli
P32156
-
-
5.4.99.62
Escherichia coli
P04982
-
-
Purification (Commentary)
EC Number
Commentary
Organism
5.1.3.29
-
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.1.3.29
alpha-L-fucopyranose
-
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
5.1.3.29
alpha-L-fucopyranose
FucU binds to both alpha- and beta-fucopyranose and accelerates the conversion between them
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
5.1.3.29
additional information
FucU exhibits a pyranase activity for D-ribose. No activity with D-glucose, L-rhamnose and D-fucose
725359
Escherichia coli
?
-
-
-
-
5.1.3.32
alpha-L-rhamnopyranose
-
725359
Escherichia coli
beta-L-rhamnopyranose
-
-
-
?
5.1.3.32
alpha-L-rhamnopyranose
the enzyme is specific for L-rhamnopyranose
725359
Escherichia coli
beta-L-rhamnopyranose
-
-
-
?
5.4.99.62
beta-allopyranose
-
725359
Escherichia coli
beta-allofuranose
-
-
-
?
5.4.99.62
beta-D-ribopyranose
-
725359
Escherichia coli
beta-D-ribofuranose
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
5.1.3.29
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
5.1.3.32
More
the enzyme seems to require multimeric or dimeric structure for their enzymatic activity
Escherichia coli
5.4.99.62
More
the enzyme seems to require multimeric or dimeric structure for their enzymatic activity
Escherichia coli
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
5.1.3.29
-
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
5.4.99.62
H106A
the mutant enzyme retains one-third of the original pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does,
Escherichia coli
5.4.99.62
H20A
mutation completely abolishes the pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does,
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5.1.3.29
alpha-L-fucopyranose
Escherichia coli
-
beta-L-fucopyranose
-
-
r
5.1.3.32
alpha-L-rhamnopyranose
Escherichia coli
-
beta-L-rhamnopyranose
-
-
?
5.4.99.62
beta-D-ribopyranose
Escherichia coli
-
beta-D-ribofuranose
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
5.1.3.29
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.1.3.29
alpha-L-fucopyranose
-
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
5.1.3.29
alpha-L-fucopyranose
FucU binds to both alpha- and beta-fucopyranose and accelerates the conversion between them
725359
Escherichia coli
beta-L-fucopyranose
-
-
-
r
5.1.3.29
additional information
FucU exhibits a pyranase activity for D-ribose. No activity with D-glucose, L-rhamnose and D-fucose
725359
Escherichia coli
?
-
-
-
-
5.1.3.32
alpha-L-rhamnopyranose
-
725359
Escherichia coli
beta-L-rhamnopyranose
-
-
-
?
5.1.3.32
alpha-L-rhamnopyranose
the enzyme is specific for L-rhamnopyranose
725359
Escherichia coli
beta-L-rhamnopyranose
-
-
-
?
5.4.99.62
beta-allopyranose
-
725359
Escherichia coli
beta-allofuranose
-
-
-
?
5.4.99.62
beta-D-ribopyranose
-
725359
Escherichia coli
beta-D-ribofuranose
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
5.1.3.29
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
5.1.3.32
More
the enzyme seems to require multimeric or dimeric structure for their enzymatic activity
Escherichia coli
5.4.99.62
More
the enzyme seems to require multimeric or dimeric structure for their enzymatic activity
Escherichia coli
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5.1.3.29
27.9
-
alpha-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
5.1.3.29
65.1
-
beta-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
5.1.3.29
27.9
-
alpha-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli
5.1.3.29
65.1
-
beta-L-fucopyranose
pH 7.5, temperature not specified in the publication
Escherichia coli