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Information on EC 5.1.3.8 - N-acylglucosamine 2-epimerase

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.8 N-acylglucosamine 2-epimerase
IUBMB Comments
Requires catalytic amounts of ATP.
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This record set is specific for:
UNIPROT: A4UA16
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glcnac 2-epimerase, renin-binding protein, anage, n-acetyl-d-glucosamine 2-epimerase, n-acyl-d-glucosamine 2-epimerase, renin binding protein, n-acetylglucosamine 2-epimerase, avaage, bglcnac 2-epimerase, n-acylglucosamine 2-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bGlcNAc 2-epimerase
recombinant protein
GlcNAc 2-epimerase
-
GlcNAc-2-epimerase
-
N-acetyl-D-glucosamine-2-epimerase
-
N-acyl-D-glucosamine 2-epimerase
-
N-acylglucosamine 2-epimerase
-
Acylglucosamine 2-epimerase
-
-
-
-
Epimerase, acylglucosamine 2-
-
-
-
-
GlcNAc 2-epimerase
-
-
-
-
N-acetyl-D-glucosamine 2-epimerase
-
-
-
-
N-Acetylglucosamine 2-epimerase
-
-
-
-
Renin-binding protein
-
-
-
-
RNBP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
N-Acyl-D-glucosamine 2-epimerase
Requires catalytic amounts of ATP.
CAS REGISTRY NUMBER
COMMENTARY hide
37318-34-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosamine
N-acetyl-D-mannosamine
show the reaction diagram
-
-
-
r
N-acetyl-D-mannosamine
N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
r
N-Acyl-D-glucosamine
N-Acyl-D-mannosamine
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosamine
N-acetyl-D-mannosamine
show the reaction diagram
-
-
-
r
N-Acyl-D-glucosamine
N-Acyl-D-mannosamine
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
no effect
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyruvate
50% reduced activity at 0.2 M pyruvate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
20 fold increase in activity
AMPPNP
20 fold increase in activity
ATP
20 fold increase in activity, 0.020 mM for maximal activity
dATP
20 fold increase in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2 - 45.7
N-acetyl-D-glucosamine
9.2 - 57.33
N-acetyl-D-mannosamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
123.8
wild type, reverse conversion in the presence of 1 mM ATP
124
in the presence of 1 mM ATP
22.8
E218A, in the presence of 1 mM ATP
256.4
E218D, in the presence of 1 mM ATP
258.5
N179A, in the presence of 1 mM ATP
351
C370A, in the presence of 1 mM ATP
46.5
E218D, reverse conversion in the presence of 1 mM ATP
5.6
E242Q, reverse conversion in the presence of 1 mM ATP
50.8
N179A, reverse conversion in the presence of 1 mM ATP
525.8
wild type, in the presence of 1 mM ATP
54.8
R375A, in the presence of 1 mM ATP
6.2
R375A, reverse conversion in the presence of 1 mM ATP
6.6
E218A, reverse conversion in the presence of 1 mM ATP
8.1
E242Q, in the presence of 1 mM ATP
8.9
R375K, reverse conversion in the presence of 1 mM ATP
85.9
C370A, reverse conversion in the presence of 1 mM ATP
94.3
R375K, in the presence of 1 mM ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 55
more than 90% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A4UA16_9NOST
388
0
45062
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
calculated, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of its apoform
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C370A
site directed mutagenesis
E218A
site directed mutagenesis
E218D
site directed mutagenesis
E242Q
site directed mutagenesis
E308A
site directed mutagenesis
E308D
site directed mutagenesis
H239A
site directed mutagenesis
H239N
site directed mutagenesis
H372A
site directed mutagenesis
H372I
site directed mutagenesis
H372N
site directed mutagenesis
N179A
site directed mutagenesis
R375A
site directed mutagenesis
R375K
site directed mutagenesis
R57A
site directed mutagenesis
R57K
site directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the recombinant protein by immobilized nickel-ion chromatography
of the recombinant proteins, wild type and mutants by immobilized nickel-ion chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, copurification with recombinant Escherichia coli N-acetyl-D-neuraminic acid aldolase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene bage, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), coexpression with N-acetyl-D-neuraminic acid aldolase gene nanA from Escherichia coli
recombinant enzyme expression in Escherichia coli, coexpression with N-acetylneuraminic acid lyase from Corynebacterium glutamicum ATCC 13032 (CgNal, EC 4.1.3.3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
recombinant Escherichia coli cells synchronously expressing N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid aldolase as biocatalysts can potentially be used in the industrial mass production of Neu5Ac
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, Y.C.; Chien, H.C.; Hsu, W.H.
Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase
J. Biotechnol.
129
453-460
2007
Anabaena sp. CH1 (A4UA16), Sus scrofa (P17560), Sus scrofa
Manually annotated by BRENDA team
Lee, Y.C.; Wu, H.M.; Chang, Y.N.; Wang, W.C.; Hsu, W.H.
The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion
J. Mol. Biol.
367
895-908
2007
Anabaena sp. CH1 (A4UA16)
Manually annotated by BRENDA team
Wang, Z.; Zhuang, W.; Cheng, J.; Sun, W.; Wu, J.; Chen, Y.; Ying, H.
In vivo multienzyme complex coconstruction of N-acetylneuraminic acid lyase and N-acetylglucosamine-2-epimerase for biosynthesis of N-acetylneuraminic acid
J. Agric. Food Chem.
65
7467-7475
2017
Anabaena sp. CH1 (A4UA16)
Manually annotated by BRENDA team
Kao, C.H.; Chen, Y.Y.; Wang, L.R.; Lee, Y.C.
Production of N-acetyl-D-neuraminic acid by recombinant single whole cells co-expressing N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid aldolase
Mol. Biotechnol.
60
427-434
2018
Anabaena sp. CH1 (A4UA16)
Manually annotated by BRENDA team