Information on EC 5.1.3.24 - N-acetylneuraminate epimerase

for references in articles please use BRENDA:EC5.1.3.24
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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
COMMENTARY hide
5.1.3.24
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RECOMMENDED NAME
GeneOntology No.
N-acetylneuraminate epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
N-acetyl-alpha-neuraminate 2-epimerase
Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages and are released in alpha form during degradation. This enzyme accelerates maturotation to the beta form (which also occurs as a slow spontaneous reaction), which is necessary for further metabolism by the bacteria.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha-neuraminate
N-acetyl-beta-neuraminate
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha-neuraminate
N-acetyl-beta-neuraminate
show the reaction diagram
P39371
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38685
2 * 38685, electrospray mass spectrometry
73900
equilibrium sedimentation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 38685, electrospray mass spectrometry
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, 1.5 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E325A
mutation has no effect on the activity
H278A
mutation has no effect on the activity
K11A
mutation has no effect on the activity
K283A
mutation has no effect on the activity
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
Y309A
mutation has no effect on the activity
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Show AA Sequence (678 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 5.1.3.24)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)