Information on EC 5.1.3.24 - N-acetylneuraminate epimerase:
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The lowest common taxonomy group for this enzyme is: Escherichia coli

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EC NUMBERCOMMENTARY
5.1.3.24-

RECOMMENDED NAMEGeneOntology No.
N-acetylneuraminate epimerase-

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
N-acetyl-alpha-neuraminate 2-epimeraseSialoglycoconjugates 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.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
N-acetylneuraminate mutarotase----
N-acetylneuraminate mutarotaseEscherichia coliP39371-715495
sialic acid epimerase----
sialic acid epimeraseEscherichia coliP39371-715495
YjhT----
YjhTEscherichia coliP39371-715495

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Escherichia coli-715495P39371SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEscherichia coliP39371probably 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 responses715495

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha-neuraminateN-acetyl-beta-neuraminate
show the reaction diagram		Escherichia coliP39371probably 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, the enzyme converts alpha-N-acetylneuranimic acid to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers715495--?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
N-acetyl-alpha-neuraminateN-acetyl-beta-neuraminate
show the reaction diagram		Escherichia coliP39371probably 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 responses715495--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
periplasmEscherichia coliP39371--715495Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
73900-Escherichia coliP39371equilibrium sedimentation715495

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerEscherichia coliP393712 * 38685, electrospray mass spectrometry715495

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
vapor diffusion method, 1.5 A resolutionEscherichia coliP39371715495

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coliP39371715495

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliEscherichia coliP39371715495

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
E209AEscherichia coliP39371the 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 YjhT715495
E325AEscherichia coliP39371mutation has no effect on the activity715495
H278AEscherichia coliP39371mutation has no effect on the activity715495
K11AEscherichia coliP39371mutation has no effect on the activity715495
K283AEscherichia coliP39371mutation has no effect on the activity715495
R215AEscherichia coliP39371mutant 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 YjhT715495
Y309AEscherichia coliP39371mutation has no effect on the activity715495

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
715495Severi, E.; Müller, A.; Potts, J.R.; Leech, A.; Williamson, D.; Wilson, K.S.; Thomas, G.H.Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhTJ. Biol. Chem.2834841-48492008Escherichia coli PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.1.3.24)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)