Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase and Organism(s) Arabidopsis thaliana and UniProt Accession O64765

for references in articles please use BRENDA:EC2.7.7.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: O64765
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
UDP-N-acetylglucosamine diphosphorylase 2
-
acetylglucosamine 1-phosphate uridylyltransferase
-
-
-
-
GlmU
-
-
-
-
UDP-GlcNAc pyrophosphorylase
-
-
-
-
UDP-HexNAc pyrophosphorylase
-
-
-
-
UDP-N-acetylglucosamine diphosphorylase 1
-
UDPacetylglucosamine pyrophosphorylase
-
-
-
-
uridine diphosphate-N-acetylglucosamine pyrophosphorylase
-
-
-
-
uridine diphosphoacetylglucosamine phosphorylase
-
-
-
-
uridine diphosphoacetylglucosamine pyrophosphorylase
-
-
-
-
UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase
-
-
-
-
Ydl103c protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
-
-
-
r
UDP-N-acetyl-D-galactosamine + diphosphate
N-acetyl-D-galactosamine 1-phosphate + UTP
show the reaction diagram
-
-
-
r
UDP-N-acetyl-D-glucosamine + diphosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
show the reaction diagram
-
-
-
r
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
-
-
-
r
UDP-N-acetyl-D-galactosamine + diphosphate
N-acetyl-D-galactosamine 1-phosphate + UTP
show the reaction diagram
-
-
-
r
UDP-N-acetyl-D-glucosamine + diphosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
show the reaction diagram
-
-
-
r
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
or Mn2+, required
Mn2+
or Mg2+, required
Mg2+
or Mn2+, required
Mn2+
or Mg2+, required. At 5 mM, 126% of the activity with Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
0.5 mM, 56% reduction in activity
EDTA
5 mM, 11% residual activity
hygromycin
0.5 mg/ml, 36% reduction in activity
streptomycin
0.5 mg/ml, 74% reduction in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
N-acetyl-D-glucosamine 1-phosphate
pH 7.6, 37°C
0.808
UDP-N-acetyl-D-galactosamine
pH 7.6, 37°C
0.065
UDP-N-acetyl-D-glucosamine
pH 7.6, 37°C
0.203
UTP
pH 7.6, 37°C
0.337
N-acetyl-D-glucosamine 1-phosphate
pH 7.6, 37°C
2.768
UDP-N-acetyl-D-galactosamine
pH 7.6, 37°C
0.219
UDP-N-acetyl-D-glucosamine
pH 7.6, 37°C
0.296
UTP
pH 7.6, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
160
N-acetyl-D-glucosamine 1-phosphate
pH 7.6, 37°C
18
UDP-N-acetyl-D-galactosamine
pH 7.6, 37°C
460
UDP-N-acetyl-D-glucosamine
pH 7.6, 37°C
140
UTP
pH 7.6, 37°C
110
N-acetyl-D-glucosamine 1-phosphate
pH 7.6, 37°C
15
UDP-N-acetyl-D-galactosamine
pH 7.6, 37°C
220
UDP-N-acetyl-D-glucosamine
pH 7.6, 37°C
120
UTP
pH 7.6, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform GLCNAC1PUT2
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UAP2_ARATH
502
0
55760
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, SDS-PAGE
58300
1 * 58300, SDS-PAGE
60000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, SDS-PAGE
monomer
1 * 58300, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1
generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, T.; Echols, M.; Martin, A.; Bar-Peled, M.
Identification and characterization of a strict and a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis
Biochem. J.
430
275-284
2010
Arabidopsis thaliana (O64765), Arabidopsis thaliana (Q940S3)
Manually annotated by BRENDA team