|Gene:||nagA||Accession Number: G-14699 (MetaCyc)|
Species: Vibrio cholerae non-O1
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].
|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]
|Cellular Component:||GO:0005829 - cytosol [Yamano96]|
Enzymatic reaction of: N-acetylglucosamine-6-phosphate deacetylase
EC Number: 188.8.131.52
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.
In Pathways: chitin derivatives degradation
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].
T(opt): 37 °C [Yamano96]
pH(opt): 7.8-8.5 [Yamano96]
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
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