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Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase and Organism(s) Escherichia coli and UniProt Accession P0ACC7

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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 .
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Escherichia coli
UNIPROT: P0ACC7
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-n-acetylglucosamine pyrophosphorylase, lmuap1, glmumtb, spl29, udp-n-acetylglucosamine pyrophosphorylase (uap), glcnac-1-p utase, udp-n-acetylglucosamine pyrophosphorylase 1, n-acetylglucosamine 1-phosphate uridyltransferase, agx-1, udp-n-acetylhexosamine pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GlcNAc-1-P UTase
-
N-acetylglucosamine-1-phosphate uridyltransferase
-
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
acetylglucosamine 1-phosphate uridylyltransferase
-
-
-
-
N-acetylglucosamine 1-phosphate uridyltransferase
-
-
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
-
UDP-GlcNAc pyrophosphorylase
-
-
-
-
UDP-HexNAc pyrophosphorylase
-
-
-
-
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
-
-
-
-
additional information
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
CTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + CDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
?
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
-
-
-
?
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
N-acetyl-4-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-4-deoxy-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 59%
-
?
N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 20%
-
?
N-acetyl-6-deoxy-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-galactosamine + diphosphate
show the reaction diagram
-
-
yield: 55%
-
?
N-acetyl-6-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 50%
-
?
N-acetyl-alpha-D-allopyranosylamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-allopyranosylamine + diphosphate
show the reaction diagram
-
-
yield: 20%
-
?
N-acetyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-galactosamine + diphosphate
show the reaction diagram
-
-
yield: 65%
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 40%
-
?
N-azidoacetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-azidoacetyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 44%
-
?
N-butanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-butanoyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 27%
-
?
N-propanoyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-galactosamine + diphosphate
show the reaction diagram
-
-
yield: 10%
-
?
N-propanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-glucosamine + diphosphate
show the reaction diagram
-
-
yield: 57%
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
additional information
?
-
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
-
-
-
?
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
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
binds to enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl) phenylamino]-2-(-4-pyridyl)-1-ethanone
commercial inhibitor
UDP-N-acetyl-D-glucosamine
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slight product inhibition in reverse reaction
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
N-acetyl-D-glucosamine 1-phosphate
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pH 8.2, 37°C
0.1
UTP
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pH 8.2, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 330
N-acetyl-D-glucosamine 1-phosphate
44.3
UDP-N-acetyl-D-glucosamine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52.56
mutant enzyme Y103V, 37°C, pH 7.5
75.63
wild-type enzyme, 37°C, pH 7.5
93.97
mutant enzyme Y103A, 37°C, pH 7.5
99.8
mutant enzyme Y103N, 37°C, pH 7.5
15.1
-
purified enzyme, pH 8.2, 37°C
20.4
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
inactivation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
additional information
the Tyr103-Asp105 segment is located at the floor of the uridyltransferase active pocket and is involved in interactions with UTP and GlcNAc-1-P substrates
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24700
-
SDS-PAGE, enzyme variant del233
25600
-
SDS-PAGE, enzyme variant del227
28600
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SDS-PAGE, enzyme variant Tr250
36200
-
SDS-PAGE, enzyme variant del130
37100
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SDS-PAGE, Tr331
41800
-
SDS-PAGE, enzyme variant del78
49000
-
SDS-PAGE, corresponds very well with molecular weight expected from DNA sequence
50100
-
SDS-PAGE, calculated from DNA sequence
53000
-
SDS-PAGE, His-Tag contributed with 3900 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction
trimer
trimer
-
3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, hanging drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D105A
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
E154D
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme
E154K
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 90% reduced activity compared to the wild-type enzyme
E154L
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 70% reduced activity compared to the wild-type enzyme
N169A
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 50% reduced activity compared to the wild-type enzyme
N169D
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme
N169Q
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme
N169R
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows 1.4fold increased activity compared to the wild-type enzyme. The N169R mutant caused a slightly secondary structure changes, thus facilitating GlcNAc-1-phosphate to enter the active pocket through the additional interaction with N-acetyl arm of GlcNAc moiety
Q76A
site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview
Q76E
site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview
Q76P
site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview
T82G
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 65% reduced activity compared to the wild-type enzyme
T82Q
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme
T82S
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme
Y103A
Y103F
site-directed mutagenesis of the residue located nearby the uridyltransferase active pocket,the mutant shows increased activity compared to the wild-type enzyme
Y103N
Y103V
mutant protein shows a 30% decrease in activity compared to that of the wild-type enzyme
DELTA1-130
-
deletion of N-terminus, very low activity
DELTA1-182
-
deletion of N-terminus, very low activity
DELTA1-227
-
deletion of N-terminus, very low activity
DELTA1-233
-
deletion of N-terminus, very low activity
DELTA1-250
-
deletion of N-terminus
DELTA1-26
-
deletion of N-terminus
DELTA1-78
-
deletion of N-terminus, very low activity
DELTA227-456
-
deletion of C-terminus
DELTA250-456
-
deletion of C-terminus, low activity
DELTA331-456
-
deletion of C-terminus, roughly 50% of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
completely insensitive to millimolar concentrations of thiol reagents
-
dithiothreitol increases thermal stability
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 month, 10% loss of activity
-
25°C, 1 mM dithiothreitol, 1 mM N-acetyl-D-glucosamine 1-phosphate, 20h, 30% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
full length and truncated enzymes using His-tag
-
His-tag used for purifcation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene glmU, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene glmU, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
-
overexpressed in Escherichia coli, His-tag inserted for purification
-
overexpression in host strain
-
truncated and full length enzyme overexpressed in Escherichia coli, His-tag inserted for purification
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
potential target for antibacterial agents
synthesis
-
synthesis of UDP-N-acetyl-D-glucosamine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mengin-Lecreulx, D.; van Heijenoort, J.
Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
J. Bacteriol.
176
5788-5795
1994
Escherichia coli
Manually annotated by BRENDA team
Pompeo, F.; Bourne, Y.; Van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth
J. Biol. Chem.
276
3833-3839
2001
Escherichia coli
Manually annotated by BRENDA team
De Luca, C.; Lansing, M.; Crescenzi, F.; Martini, I.; Shen, G.J.; O'Regan, M.; Wong, C.H.
Overexpression, one-step purification and characterization of UDP-glucose dehydrogenase and UDP-N-acetylglucosamine pyrophosphorylase
Bioorg. Med. Chem.
4
131-141
1996
Escherichia coli
Manually annotated by BRENDA team
Sulzenbacher, G.; Gal, L.; Peneff, C.; Fassy, F.; Bourne, Y.
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture
J. Biol. Chem.
276
11844-11851
2001
Escherichia coli (P0ACC7), Streptococcus pneumoniae (Q97R46), Streptococcus pneumoniae
Manually annotated by BRENDA team
Shao, J.; Zhang, J.; Nahalka, J.; Wang, P.G.
Biocatalytic synthesis of uridine 5'-diphosphate N-acetylglucosamine by multiple enzymes co-immobilized on agarose beads
Chem. Commun. (Camb.)
2002
2586-2587
2002
Escherichia coli
-
Manually annotated by BRENDA team
Olsen, L.R.; Roderick, S.L.
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
Biochemistry
40
1913-1921
2001
Escherichia coli (P0ACC7)
Manually annotated by BRENDA team
Brown, K.; Pompeo, F.; Dixon, S.; Mengin-Lecreulx, D.; Cambillau, C.; Bourne, Y.
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily
EMBO J.
18
4096-4107
1999
Escherichia coli
Manually annotated by BRENDA team
Guan, W.; Cai, L.; Fang, J.; Wu, B.; George Wang, P.
Enzymatic synthesis of UDP-GlcNAc/UDP-GalNAc analogs using N-acetylglucosamine 1-phosphate uridyltransferase (GlmU)
Chem. Commun. (Camb. )
2009
6976-6978
2009
Escherichia coli
Manually annotated by BRENDA team
Trempe, J.F.; Shenker, S.; Kozlov, G.; Gehring, K.
Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli
Protein Sci.
20
745-752
2011
Escherichia coli (P0ACC7)
Manually annotated by BRENDA team
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU)
Appl. Microbiol. Biotechnol.
100
3071-3085
2015
Escherichia coli (P0ACC7), Escherichia coli ATCC 25922 (P0ACC7)
Manually annotated by BRENDA team
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
J. Biomol. Screen.
21
342-353
2016
Escherichia coli (P0ACC7), Escherichia coli ATCC 25922 (P0ACC7)
Manually annotated by BRENDA team
Wang, S.; Fu, X.; Liu, Y.; Liu, X.W.; Wang, L.; Fang, J.; Wang, P.G.
Probing the roles of conserved residues in uridyltransferase domain ofEscherichia coli K12 GlmU by site-directed mutagenesis
Carbohydr. Res.
413
70-74
2015
Escherichia coli (P0ACC7)
Manually annotated by BRENDA team
Honda, Y.; Zang, Q.; Shimizu, Y.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position
Appl. Environ. Microbiol.
83
e02291
2017
Escherichia coli (P0ACC7), Escherichia coli K12 (P0ACC7), Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
Honda, Y.; Zang, Q.; Shimizu, Y.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position
Appl. Environ. Microbiol.
83
e02291-16
2017
Escherichia coli (P0ACC7), Escherichia coli K12 (P0ACC7), Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Manually annotated by BRENDA team
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU)
Appl. Microbiol. Biotechnol.
100
3071-3085
2016
Escherichia coli, Escherichia coli ATCC 25922
Manually annotated by BRENDA team
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
J. Biomol. Screen.
21
342-353
2016
Escherichia coli (P0ACC7), Escherichia coli ATCC 25922 (P0ACC7)
Manually annotated by BRENDA team