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2.3.1.157: glucosamine-1-phosphate N-acetyltransferase

This is an abbreviated version!
For detailed information about glucosamine-1-phosphate N-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.157

Reaction

acetyl-CoA
+
alpha-D-glucosamine 1-phosphate
=
CoA
+
N-acetyl-alpha-D-glucosamine 1-phosphate

Synonyms

amino-sugar-1-P AcTase, amino-sugar-1-phosphate acetyltransferase, bifunctional GlmU protein, bifunctional N-acetyltransferase/uridylyltransferase, bifunctional protein GlmU, bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase, galactosamine-1-phosphate acetyltransferase, GalN-1-P AcTase, GlcN-1-P acetyltransferase, GlcN-1-P AcTase, GlcNAc-1-P uridyltransferase, GlmU, GlmU acetyltransferase, GlmU enzyme, GlmU uridyltransferase, glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase, glucosamine-1-phosphate acetyltransferase, glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase, More, MtbGlmU, MtGlmU, N-acetylglucosamine-1-phosphate pyrophosphorylase, N-acetylglucosamine-1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase, N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase, Rv1018c, Rxn-1, ST0452, ST0452 protein, STK_04520, UDP-GlcNAc pyrophosphorylase, UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.157 glucosamine-1-phosphate N-acetyltransferase

Temperature Stability

Temperature Stability on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble by 5-min treatment at 80 °C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein