2.3.1.276: galactosamine-1-phosphate N-acetyltransferase
This is an abbreviated version!
For detailed information about galactosamine-1-phosphate N-acetyltransferase, go to the full flat file.
Reaction
Synonyms
Gal-1-P AcTase, galactosamine-1-phosphate acetyltransferase, GalN-1-P AcTase, ST0452
ECTree
2.3.1.276 galactosamine-1-phosphate N-acetyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.276 - galactosamine-1-phosphate N-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H308A
specific activity is 7.7% compared to the wild-type enzyme
K340A
specific activity is 63.3% compared to the wild-type enzyme
K377A
specific activity is 82.6% compared to the wild-type enzyme
N331A
specific activity is 3.1% compared to the wild-type enzyme
T80S/Y97N
the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity
Y311A
specific activity is 3.3% compared to the wild-type enzyme
Y97N
additional information
C-terminal deletion mutants DC005 and DC011 (deletion of the C-terminal 5 or 11 residues of the ST0452 protein) shows 20% and 38% less galactosamine-1-phosphate acetyltransferase activity than the wild-type ST0452 protein. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability 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. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C
Y97N
the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein was not changed by this substitution but the interactions with the substrate were slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
Y97N
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the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein was not changed by this substitution but the interactions with the substrate were slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
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