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EC Tree
IUBMB Comments Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate .
The taxonomic range for the selected organisms is: Candida albicans The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-n-acetylglucosamine pyrophosphorylase, lmuap1, glmumtb, udp-n-acetylglucosamine pyrophosphorylase (uap), glcnac-1-p utase, spl29, udp-n-acetylglucosamine pyrophosphorylase 1, n-acetylglucosamine 1-phosphate uridyltransferase, agx-1, lmuap2,
more
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N-acetylglucosamine-1-phosphate uridyltransferase
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acetylglucosamine 1-phosphate uridylyltransferase
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UDP-GlcNAc pyrophosphorylase
UDP-GlcNAc pyrophosphorylase (UAP)
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UDP-HexNAc pyrophosphorylase
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UDP-N-acetylglucosamine pyrophosphorylase (UAP)
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UDPacetylglucosamine pyrophosphorylase
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uridine diphosphate-N-acetylglucosamine pyrophosphorylase
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uridine diphosphoacetylglucosamine phosphorylase
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uridine diphosphoacetylglucosamine pyrophosphorylase
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uridine-diphospho-N-acetylglucosamine pyrophosphorylase
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UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase
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GlmU
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UDP-GlcNAc pyrophosphorylase
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UDP-GlcNAc pyrophosphorylase
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nucleotidyl group transfer
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UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
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diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
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r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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?
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
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the reaction proceeds as an SN2 reaction
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r
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
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N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
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r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
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r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
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r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
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r
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diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
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N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
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r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
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r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
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r
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Mg2+
strictly required. One magnesium ion catalyzes the sugar-nucleotidyl transfer reaction. 5 mM used in assay conditions
Ca2+
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Ca2+
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Ca2+ shows similar enhancement like Mg2+
Mg2+
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Mg2+
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Mg2+ enhances the enzymatic activity by increasing the affinity between UTP and the enzyme
Zn2+
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Zn2+
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Zn2+ shows similar enhancement like Mg2+
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Uniprot
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UAP1_CANAX
486
0
54644
Swiss-Prot
other Location (Reliability: 2 )
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hanging drop vapour diffusion method
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sitting-drop vapour-diffusion method
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K421A
the activity of the mutant is very low (less than 5%) in comparison to the wild type enzyme
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GST fusion protein from E. coli
glutathione Sepharose column chromatography and Superdex 75 gel filtration
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expressed in Escherichia coli as GST fusion protein, complementation of Saccharomyces cerevisiae deficiency mutant, all recombinant enzymes found to be active
expressed in Escherichia coli JM109 cells as a glutathione S-transferase fusion protein
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Mio, T.; Yabe, T.; Arisawa, M.; Yamada-Okabe, H.
The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism
J. Biol. Chem.
273
14392-14397
1998
Candida albicans (O74933), Candida albicans, Homo sapiens, Saccharomyces cerevisiae (P43123), Saccharomyces cerevisiae
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Maruyama, D.; Nishitani, Y.; Nonaka, T.; Kita, A.; Fukami, T.A.; Mio, T.; Yamada-Okabe, H.; Yamada-Okabe, T.; Miki, K.
Purification, crystallization and preliminary X-ray diffraction studies of UDP-N-acetylglucosamine pyrophosphorylase from Candida albicans
Acta Crystallogr. Sect. F
62
1206-1208
2006
Candida albicans
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Maruyama, D.; Nishitani, Y.; Nonaka, T.; Kita, A.; Fukami, T.A.; Mio, T.; Yamada-Okabe, H.; Yamada-Okabe, T.; Miki, K.
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism
J. Biol. Chem.
282
17221-17230
2007
Candida albicans
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Bais, V.S.; Aggarwal, P.; Bharadwaj, P.; Prakash, B.
Classification, characterization and structural analysis of sugar nucleotidylyltransferase family of enzymes
Biochem. Biophys. Res. Commun.
525
780-785
2020
Candida albicans (O74933), Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3)
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