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NAGK encodes a member of the N-acetylhexosamine kinase family.
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results indicate that the NAGK-dynein interaction with the involvements of Lis1 (show PAFAH1B1 Antibodies) and NudE1 plays an important role in prophase nuclear envelope breakdown (NEB (show NEB Antibodies)) and metaphase MT-KT attachment during eukaryotic cell division.
Data shows associations between NAGK, speckle, paraspeckle and general transcription factor suggesting its regulatory roles in gene expression.
Participants with homozygous mutations in the N-acetylmannosamine kinase (GNK) domain have an earlier disease onset than heterozygous participants with mutations in the uridine diphosphate-N-acetylglucosamine 2-epimerase (GNE (show GNE Antibodies)) and GNK domains.
The cell-free system was validated for MNK activity, and it revealed that mutations in one enzymatic domain (in MNK, A631V, M712T) affected not only that domain's enzyme activity, but also the activity of the other domain.
Phosphorylation of Tyr205 may modulate GlcNAc kinase activity and/or specificity.
Data show that the non-conserved C-terminus of Synechococcus elongatus N-acetylglutamate kinase (NAGK) enhances arginine inhibition and holds most of the differences between S. elongatus and Arabidopsis NAGK with respect to arginine sensitivity.
These results reveal a complex metabolic control of the PII interaction with NAGK in the chloroplast stroma of higher plants.
This gene encodes a member of the N-acetylhexosamine kinase family. The encoded protein catalyzes the conversion of N-acetyl-D-glucosamine to N-acetyl-D-glucosamine 6-phosphate, and is the major mammalian enzyme which recovers amino sugars.
, glcNAc kinase
, GlcNAc kinase
, N-acetylglucosamine kinase
, n-acetylglucosamine kinase