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Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase and Organism(s) Candida albicans and UniProt Accession O74933

for references in articles please use BRENDA:EC2.7.7.23
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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 .
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Candida albicans
UNIPROT: O74933
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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, glcnac-1-p utase, spl29, udp-n-acetylglucosamine pyrophosphorylase (uap), udp-n-acetylglucosamine pyrophosphorylase 1, n-acetylglucosamine 1-phosphate uridyltransferase, agx-1, udp-n-acetylhexosamine pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acetylglucosamine-1-phosphate uridyltransferase
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acetylglucosamine 1-phosphate uridylyltransferase
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UAP enzyme
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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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Ydl103c protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-06-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
show the reaction diagram
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-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
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-
-
?
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
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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
show the reaction diagram
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-
-
-
?
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
show the reaction diagram
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-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
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-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
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-
-
-
?
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
show the reaction diagram
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-
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-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
strictly required. One magnesium ion catalyzes the sugar-nucleotidyl transfer reaction. 5 mM used in assay conditions
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UAP1_CANAX
486
0
54644
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
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sitting-drop vapour-diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K421A
the activity of the mutant is very low (less than 5%) in comparison to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GST fusion protein from E. coli
glutathione Sepharose column chromatography and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team