BRENDA - Enzyme Database show
show all sequences of 5.1.3.24

Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT

Severi, E.; Müller, A.; Potts, J.R.; Leech, A.; Williamson, D.; Wilson, K.S.; Thomas, G.H.; J. Biol. Chem. 283, 4841-4849 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
vapor diffusion method, 1.5 A resolution
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
E209A
the mutant of YjhT is severely impaired in its ability to enhance the mutarotation rate above the spontaneous rate. Circular dichroism spectrum of the mutant is indistinguishable from that of the wild-type protein, suggesting that the phenotype is not because of misfolding of YjhT
Escherichia coli
E325A
mutation has no effect on the activity
Escherichia coli
H278A
mutation has no effect on the activity
Escherichia coli
K11A
mutation has no effect on the activity
Escherichia coli
K283A
mutation has no effect on the activity
Escherichia coli
R215A
mutant shows a decreased but observable activity. Circular dichroism spectrum of the mutant is indistinguishable from that of the wild-type protein, suggesting that the phenotype is not because of misfolding of YjhT
Escherichia coli
Y309A
mutation has no effect on the activity
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Escherichia coli
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38685
-
2 * 38685, electrospray mass spectrometry
Escherichia coli
73900
-
equilibrium sedimentation
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-acetyl-alpha-neuraminate
Escherichia coli
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
N-acetyl-beta-neuraminate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P39371
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-acetyl-alpha-neuraminate
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
715495
Escherichia coli
N-acetyl-beta-neuraminate
-
-
-
?
N-acetyl-alpha-neuraminate
the enzyme converts alpha-N-acetylneuranimic acid to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers
715495
Escherichia coli
N-acetyl-beta-neuraminate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 38685, electrospray mass spectrometry
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
vapor diffusion method, 1.5 A resolution
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E209A
the mutant of YjhT is severely impaired in its ability to enhance the mutarotation rate above the spontaneous rate. Circular dichroism spectrum of the mutant is indistinguishable from that of the wild-type protein, suggesting that the phenotype is not because of misfolding of YjhT
Escherichia coli
E325A
mutation has no effect on the activity
Escherichia coli
H278A
mutation has no effect on the activity
Escherichia coli
K11A
mutation has no effect on the activity
Escherichia coli
K283A
mutation has no effect on the activity
Escherichia coli
R215A
mutant shows a decreased but observable activity. Circular dichroism spectrum of the mutant is indistinguishable from that of the wild-type protein, suggesting that the phenotype is not because of misfolding of YjhT
Escherichia coli
Y309A
mutation has no effect on the activity
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Escherichia coli
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38685
-
2 * 38685, electrospray mass spectrometry
Escherichia coli
73900
-
equilibrium sedimentation
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-acetyl-alpha-neuraminate
Escherichia coli
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
N-acetyl-beta-neuraminate
-
-
?
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
N-acetyl-alpha-neuraminate
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
715495
Escherichia coli
N-acetyl-beta-neuraminate
-
-
-
?
N-acetyl-alpha-neuraminate
the enzyme converts alpha-N-acetylneuranimic acid to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers
715495
Escherichia coli
N-acetyl-beta-neuraminate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 38685, electrospray mass spectrometry
Escherichia coli
General Information
General Information
Commentary
Organism
physiological function
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
Escherichia coli
Other publictions for EC 5.1.3.24
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)
715495
Severi
Sialic acid mutarotation is ca ...
Escherichia coli
J. Biol. Chem.
283
4841-4849
2008
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