Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.25 extracted from

  • Davies, J.S.; Coombes, D.; Horne, C.R.; Pearce, F.G.; Friemann, R.; North, R.A.; Dobson, R.C.J.
    Functional and solution structure studies of amino sugar deacetylase and deaminase enzymes from Staphylococcus aureus (2019), FEBS Lett., 593, 52-66 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene nagA, recombinant expression in Escherichia coli strain BL21(DE3) from plasmid pET30DELTASE/nagA Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Mente kinetics. The initial rate measured for NagA has a significant substrate concentration-dependent lag phase which is not influenced by 1 mM Zn2+ and not pH-dependent Staphylococcus aureus
0.16
-
N-acetyl-D-glucosamine-6-phosphate pH 8.0, 30°C, recombinant enzyme Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ NagA requires two Zn2+ metal ions for activity Staphylococcus aureus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43200
-
recombinant reduced monomeric enzyme NagA, analytical gel filtration Staphylococcus aureus
86300
-
about, dimer, sequence calculation Staphylococcus aureus
86700
-
recombinant dimeric enzyme, analytical gel filtration Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-D-glucosamine-6-phosphate + H2O Staphylococcus aureus
-
D-glucosamine 6-phosphate + acetate
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O Staphylococcus aureus USA300_TCH1516
-
D-glucosamine 6-phosphate + acetate
-
?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-
Staphylococcus aureus USA300_TCH1516
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme NagA from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, followed by gel filtration Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information performance of a coupled assay with NagB (EC 3.5.99.6) resulting in production of fructose 6-phosphate and NH3 Staphylococcus aureus ?
-
?
additional information performance of a coupled assay with NagB (EC 3.5.99.6) resulting in production of fructose 6-phosphate and NH3 Staphylococcus aureus USA300_TCH1516 ?
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O
-
Staphylococcus aureus D-glucosamine 6-phosphate + acetate
-
?
N-acetyl-D-glucosamine-6-phosphate + H2O
-
Staphylococcus aureus USA300_TCH1516 D-glucosamine 6-phosphate + acetate
-
?

Subunits

Subunits Comment Organism
dimer NagA is an asymmetric dimer in solution, analytical ultracentrifugation and small-angle X-ray scattering data Staphylococcus aureus
More involvement of both subunits in binding substrate Staphylococcus aureus

Synonyms

Synonyms Comment Organism
NagA
-
Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Staphylococcus aureus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
345
-
N-acetyl-D-glucosamine-6-phosphate pH 8.0, 30°C, recombinant enzyme Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Staphylococcus aureus

General Information

General Information Comment Organism
metabolism N-acetylglucosamine-6-phosphate deacetylase (NagA) and glucosamine-6-phosphate deaminase (NagB) are branch point enzymes that direct amino sugars into different pathways Staphylococcus aureus
additional information involvement of both subunits in binding substrate by NagA. NagA requires two Zn2+ metal ions for activity and displays an unusual hysteretic behaviour, which may have a role in regulating flux at this step Staphylococcus aureus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2156.25
-
N-acetyl-D-glucosamine-6-phosphate pH 8.0, 30°C, recombinant enzyme Staphylococcus aureus