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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: N-acetylglucosamine-6-phosphate deacetylase

Gene: nagA Accession Number: G-14699 (MetaCyc)

Synonyms: VC0994

Species: Vibrio cholerae non-O1

Subunit composition of N-acetylglucosamine-6-phosphate deacetylase = [NagA]4
         N-acetylglucosamine-6-phosphate deacetylase subunit = NagA

Summary:
The native apparent molecular mass was determined by gel filtration chromatography [Yamano96].

This enzyme functions in the chitin catabolic cascade in Vibrio cholerae non-O1. It was purified from cell extracts and characterized [Yamano96] and the gene encoding it was cloned [Yamano97].
The subunit apparent molecular mass was determined by SDS-PAGE [Yamano96].

Locations: cytosol

Map Position: [1,059,719 <- 1,060,855]

Molecular Weight of Polypeptide: 40.956 kD (from nucleotide sequence), 45.0 kD (experimental) [Yamano96 ]

Molecular Weight of Multimer: 190.0 kD (experimental) [Yamano96]

Unification Links: Entrez-gene:2614247 , Protein Model Portal:O32445 , SMR:O32445 , String:243277.VC0994 , UniProt:O32445

Relationship Links: InterPro:IN-FAMILY:IPR003764 , InterPro:IN-FAMILY:IPR006680 , InterPro:IN-FAMILY:IPR011059 , PDB:Structure:3EGJ , PDB:Structure:3IV8 , Pfam:IN-FAMILY:PF01979

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol Inferred from experiment [Yamano96]

Credits:
Created 30-Sep-2011 by Fulcher CA , SRI International


Enzymatic reaction of: N-acetylglucosamine-6-phosphate deacetylase

EC Number: 3.5.1.25

N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Alternative Substrates for N-acetyl-D-glucosamine 6-phosphate: N-acetyl-D-glucosamine 6-sulfate [Yamano96 ] , N-acetyl-D-glucosamine [Yamano96 ]

In Pathways: chitin derivatives degradation

Summary:
Enzyme activity was assayed by measuring the amount of hexosamine produced. The temperature optimum was determined in phosphate buffer at pH 7.8. Co2+ at 4 mM activated the enzyme 200%. The enzyme also utilized N-acetyl-D-glucosamine (GlnNAc) as substrate. It did not utilize chitooligosaccharides ((GlcNAc)2-6) or N-acetyl-β-D-galactosamine as substrate [Yamano96].

Activators (Unknown Mechanism): Co2+ [Yamano96]

Inhibitors (Unknown Mechanism): N-ethylmaleimide [Yamano96] , p-chloromercuribenzoate [Yamano96] , Cu2+ [Yamano96] , EDTA [Yamano96]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
N-acetyl-D-glucosamine 6-phosphate
30.0
0.97
[Yamano96]

T(opt): 37 °C [Yamano96]

pH(opt): 7.8-8.5 [Yamano96]


References

Yamano96: Yamano N, Matsushita Y, Kamada Y, Fujishima S, Arita M (1996). "Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1." Biosci Biotechnol Biochem 60(8);1320-3. PMID: 8987551

Yamano97: Yamano N, Oura N, Wang J, Fujishima S (1997). "Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1." Biosci Biotechnol Biochem 61(8);1349-53. PMID: 9301118


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13B.