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Information on EC 2.7.7.83 - UDP-N-acetylgalactosamine diphosphorylase and Organism(s) Homo sapiens and UniProt Accession Q16222

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EC Tree
IUBMB Comments
The enzyme from plants and animals also has activity toward N-acetyl-alpha-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q16222
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Word Map
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  • 2.7.7.83
  • curl
  • whitefly
  • tabaci
  • bemisia
  • begomovirus
  • intergenic
  • geminivirus
  • viruliferous
  • virus-induced
  • geminiviridae
  • agroinoculation
  • epidemic
  • lycopersicum
  • replication-associated
  • solanum
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
galnac-1-p utase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AGX-1
UniProt
N-acetylglucosamine 1-phosphate uridyltransferase
-
UDP-N-acetylgalactosamine pyrophosphorylase
UniProt
UDP-N-acetylglucosamine pyrophosphorylase AGX1
alternatively spliced isoform to AGX2, differs from those referenced in the literature by one change: S445G (most probably a gene polymorphism)
UDP-N-acetylhexosamine pyrophosphorylase
UniProt
N-acetylglucosamine 1-phosphate uridyltransferase
-
-
UAP1
-
-
UDP-N-acetylglucosamine pyrophosphorylase AGX2
-
alternatively spliced isoform to AGX1, differs from those referenced in the literature by two changes: S445G and Q454S (most probably a gene polymorphism)
UDP-N-acetylhexosamine pyrophosphorylase AGX1
-
isoform of AGX2
UDP-N-acetylhexosamine pyrophosphorylase AGX2
-
isoform of AGX1
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:N-acetyl-alpha-D-galactosamine-1-phosphate uridylyltransferase
The enzyme from plants and animals also has activity toward N-acetyl-alpha-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].
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-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
-
-
-
r
diphosphate + UDP-N-acetylglucosamine
UTP + N-acetylglucosamine 1-phosphate
show the reaction diagram
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
AGX1
-
-
?
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
show the reaction diagram
-
-
-
r
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
show the reaction diagram
-
-
-
r
diphosphate + UDP-N-acetylglucosamine
UTP + N-acetylglucosamine 1-phosphate
show the reaction diagram
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
r
UTP + N-acetyl-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
-
r
UTP + N-acetyl-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
r
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetylglucosamine
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0053
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
0.5
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
0.032
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C
0.053
UTP
wild type protein, pH 8.0, 30°C
0.38 - 1.3
N-acetyl-D-galactosamine 1-phosphate
0.24 - 0.32
N-acetyl-D-glucosamine 1-phosphate
0.006
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
0.53
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
0.032
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C
0.049
UTP
wild type protein, pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12200
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
180
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
2000
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C
1200
UTP
wild type protein, pH 8.0, 30°C
11200
N-acetylglucosamine 1-phosphate
wild type protein, pH 8.0, 30°C
200
UDP-N-acetyl-alpha-D-galactosamine
wild type protein, pH 8.0, 30°C
2200
UDP-N-acetylglucosamine
wild type protein, pH 8.0, 30°C
1400
UTP
wild type protein, pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5
R115A mutant protein, pH 8.0, 30°C
69
wild type protein, pH 8.0, 30°C
0.119
-
GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, GST protein shows 0.02 micromol/min/mg in the assay, pH 7.5, 37°C
0.3
-
GST fusion removed, N-acetyl-D-galactosamine 1-phosphate, pH 7.5, 37°C
0.525
-
GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, GST protein shows 0.033 micromol/min/mg in the assay, pH 7.5, 37°C
0.887
-
GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, GST protein shows 0.033 micromol/min/mg in the assay, pH 7.5, 37°C
0.9
R115A mutant protein, pH 8.0, 30°C
1.342
-
GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, GST protein shows 0.02 micromol/min/mg in the assay, pH 7.5, 37°C
14.9
-
GST fusion removed, N-acety-D-lgalactosamine 1-phosphate, pH 7.5, 37°C
5.873
-
GST fusion removed, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C
5.919
-
GST fusion removed, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C
68
wild type protein, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
the human UAP1 gene encodes two different isoforms, named AGX1 and AGX2, with AGX1 being more abundant in testis and AGX2 in somatic tissues. AGX-1 is an UDP-N-acetylgalactosamine diphosphorylase, EC 2.7.7.83, and AGX-2 is an UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the naturally occuring UAP1 A229T mutation is potentially pathogenic. The A229T mutation induces structural changes, leading to reduced thermal stability and activity of the mutant compared to wild-type
additional information
the human UAP1 gene encodes two different isoforms, named AGX1 and AGX2, with AGX1 being more abundant in testis and AGX2 in somatic tissues
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UAP1_HUMAN
522
0
58769
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
gel filtration
74000
2 * 74000, gel filtration
57000
-
x * 57000, SDS-PAGE
64000
-
x * 64000, SDS-PAGE
74000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 74000, gel filtration
monomer
74000, gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged AGX1A229T in complex with UDP-GlcNAc, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement using the published AGX1 structure (PDB ID 1JV1) as a search model
vapor diffusion technique, PEG600, 20°C, pH5.7
vapor diffusion technique, PEG600, 20°C, pH5.7
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A229T
naturally occuring enzyme AGX1 mutation, and site-directed mutagenesis, the A229T mutation causes a reduction of protein thermal stability compared to wild-type AGX1, and AGX1A229T has lower activity in producing UDP-GlcNA. In diploid organisms, haploinsufficiency is a phenomenon in which a single copy of a functional gene is not sufficient to produce the normal/wild-type phenotype. The patient is only heterozygous for the UAP1 A229T missense mutation. The UAP1 gene is potentially haploinsufficient and LoF intolerant, and the heterozygous UAP1 A229T mutation is potentially pathogenic. The recombinant mutant enzyme shows a reduction of the melting temperature (Tm) by approximately 5.3°C compared to wild-type. The A229T mutation induces structural changes. The R228-E44 interaction is abolished in the AGX1A229T structure caused by the position shift of R228. The pushing effect is likely due to the bulkier side chain of threonine compared to that of alanine. Along with the conformational change of the N-terminal domain in the AGX1A229T structure, M218 is shifted by 0.8 A away from R169, weakening the Q112-R169-M218 interaction
R115A
activity drastically affected, no dimer formation
R115A
activity drastically affected
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anion exchange, phenyl interaction and gel filtration
recombinant N-terminally GST-tagged wild-type and mutant AGX1 from Escherichia coli strain (DE3) pLysS by glutathione affinity chromatography, the tag is cleaved off by PreScission protease, followed by gel filtration, and ultrafiltration
affinity chromatography (glutathione-Sepharose), GST part removed
-
anion exchange, phenyl interaction and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1 Blue
gene UAP1 encodes two different isoforms, named AGX1 and AGX2, recombinant expression of N-terminally GST-tagged wild-type and mutant AGX1 in Escherichia coli strain (DE3) pLysS
expressed in Escherichia coli XL1 Blue
GST fusion protein expressed in Escherichia coli JM109
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang-Gillam, A.; Pastuszak, I.; Elbein, A.D.
A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc
J. Biol. Chem.
273
27055-27057
1998
Homo sapiens
Manually annotated by BRENDA team
Peneff, C.; Ferrari, P.; Charrier, V.; Taburet, Y.; Monnier, C.; Zamboni, V.; Winter, J.; Harnois, M.; Fassy, F.; Bourne, Y.
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: Role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture
EMBO J.
20
6191-6202
2001
Homo sapiens, Homo sapiens (Q16222)
Manually annotated by BRENDA team
Chen, X.; Raimi, O.G.; Ferenbach, A.T.; van Aalten, D.M.F.
A missense mutation in a patient with developmental delay affects the activity and structure of the hexosamine biosynthetic pathway enzyme AGX1
FEBS Lett.
595
110-122
2020
Homo sapiens (Q16222)
Manually annotated by BRENDA team