BRENDA - Enzyme Database
show all sequences of 2.3.1.157

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

Mengin-Lecreulx, D.; van Heijenoort, J.; J. Bacteriol. 176, 5788-5795 (1994)

Data extracted from this reference:

General Stability
General Stability
Organism
acetyltransferase activity rapidly lost when the enzyme is stored in the absence of reducing thiols or acetyl coenzyme A or is treated with thiol-alkylating agents
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-Nitro-5-thiocyanobenzoic acid
-
Escherichia coli
DTNB
-
Escherichia coli
N-acetylglucosamine-1-phosphate
acetyltransferase activity inhibited by its reaction product
Escherichia coli
UDP-MurNAc
1 mM, relative enzyme activity 2%
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
N-acetyl-D-glucosamine 1-phosphate
uridyltransferase activity
Escherichia coli
0.1
-
UTP
uridyltransferase activity
Escherichia coli
0.15
-
D-glucosamine 1-phosphate
-
Escherichia coli
0.6
-
acetyl-CoA
-
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucosamine 1-phosphate + acetyl-CoA
Bacillus subtilis
-
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
Escherichia coli
-
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
Escherichia coli JM83
-
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
JM83
-
Escherichia coli JM83
-
JM83
-
Purification (Commentary)
Commentary
Organism
GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity
Escherichia coli
Reaction
Reaction
Commentary
Organism
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.2
-
GlcN-1-P acetyltransferase activity
Escherichia coli
15.1
-
GlcNAc-1-P uridyltransferase activity
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucosamine 1-phosphate + acetyl-CoA
-
288685
Bacillus subtilis
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
-
288685
Escherichia coli
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
-
288685
Escherichia coli JM83
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
-
288685
Bacillus subtilis
UDP-N-acetylglucosamine + ?
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
288685
Escherichia coli
UDP-N-acetylglucosamine + ?
-
-
-
r
N-acetyl-D-glucosamine 1-phosphate + UTP
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
288685
Escherichia coli JM83
UDP-N-acetylglucosamine + ?
-
-
-
r
UDP-N-acetylglucosamine + H2O
-
288685
Escherichia coli
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
r
UDP-N-acetylglucosamine + H2O
-
288685
Escherichia coli JM83
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
r
Subunits
Subunits
Commentary
Organism
trimer
2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
12.4
-
N-acetyl-D-glucosamine 1-phosphate
GmlU uridyltransferase
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.2
-
for both acetyltransferase and uridyltransferase
Escherichia coli
General Stability (protein specific)
General Stability
Organism
acetyltransferase activity rapidly lost when the enzyme is stored in the absence of reducing thiols or acetyl coenzyme A or is treated with thiol-alkylating agents
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-Nitro-5-thiocyanobenzoic acid
-
Escherichia coli
DTNB
-
Escherichia coli
N-acetylglucosamine-1-phosphate
acetyltransferase activity inhibited by its reaction product
Escherichia coli
UDP-MurNAc
1 mM, relative enzyme activity 2%
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
N-acetyl-D-glucosamine 1-phosphate
uridyltransferase activity
Escherichia coli
0.1
-
UTP
uridyltransferase activity
Escherichia coli
0.15
-
D-glucosamine 1-phosphate
-
Escherichia coli
0.6
-
acetyl-CoA
-
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
49000
-
gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucosamine 1-phosphate + acetyl-CoA
Bacillus subtilis
-
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
Escherichia coli
-
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
Escherichia coli JM83
-
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.2
-
GlcN-1-P acetyltransferase activity
Escherichia coli
15.1
-
GlcNAc-1-P uridyltransferase activity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucosamine 1-phosphate + acetyl-CoA
-
288685
Bacillus subtilis
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
-
288685
Escherichia coli
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
-
288685
Escherichia coli JM83
N-acetyl-D-glucosamine 1-phosphate + CoA
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
-
288685
Bacillus subtilis
UDP-N-acetylglucosamine + ?
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
288685
Escherichia coli
UDP-N-acetylglucosamine + ?
-
-
-
r
N-acetyl-D-glucosamine 1-phosphate + UTP
glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
288685
Escherichia coli JM83
UDP-N-acetylglucosamine + ?
-
-
-
r
UDP-N-acetylglucosamine + H2O
-
288685
Escherichia coli
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
r
UDP-N-acetylglucosamine + H2O
-
288685
Escherichia coli JM83
N-acetyl-D-glucosamine 1-phosphate + UMP
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
trimer
2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
12.4
-
N-acetyl-D-glucosamine 1-phosphate
GmlU uridyltransferase
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.2
-
for both acetyltransferase and uridyltransferase
Escherichia coli
Other publictions for EC 2.3.1.157
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746844
Honda
Improvement of ST0452 N-acety ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993
Appl. Environ. Microbiol.
84
e002213-18
2018
-
-
1
1
2
-
-
-
-
-
-
-
-
10
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736517
Sharma
Escherichia coli N-acetylgluco ...
Escherichia coli, Escherichia coli ATCC 25922
J. Biomol. Screen.
21
342-353
2016
-
-
1
-
-
-
3
-
-
1
-
2
-
10
-
-
1
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
4
-
2
-
-
1
1
-
-
-
2
4
4
-
-
1
-
2
-
-
-
1
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
737096
Dziadek
Mycobacterium tuberculosis Ats ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618, Mycobacterium tuberculosis H37Rv
PLoS ONE
11
e0148030
2016
-
1
1
-
1
-
-
-
-
-
-
3
-
15
-
-
1
-
-
-
-
-
6
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
729696
Zhang
Characterization of the amino ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Extremophiles
19
417-427
2015
-
1
1
-
7
-
1
9
-
1
-
6
-
8
-
-
1
-
-
-
12
-
9
2
1
-
1
6
1
-
-
1
-
-
-
-
1
1
1
-
7
-
-
1
-
9
-
1
-
6
-
-
-
1
-
-
12
-
9
2
1
-
1
6
1
-
-
-
-
2
2
-
6
6
735518
Sharma
Identification and characteriz ...
Escherichia coli, Escherichia coli ATCC 25922, Haemophilus influenzae, Haemophilus influenzae ATCC 51907
Appl. Microbiol. Biotechnol.
100
3071-3085
2015
-
-
1
-
-
-
15
-
-
-
-
8
-
12
-
-
1
-
-
-
-
-
10
-
2
-
-
-
2
-
-
2
2
-
11
-
-
1
2
-
-
-
12
17
2
-
-
-
-
8
-
-
-
1
-
-
-
-
10
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
735569
Patin
Purification and biochemical c ...
Yersinia pestis, Yersinia pestis YPIII, Yersinia pseudotuberculosis, Yersinia pseudotuberculosis YPIII
Arch. Microbiol.
197
371-378
2015
1
-
2
-
1
-
2
4
-
2
-
2
-
6
-
-
1
-
-
-
-
-
4
2
1
-
-
4
1
-
-
1
-
-
-
1
-
2
1
-
1
-
-
2
-
4
-
2
-
2
-
-
-
1
-
-
-
-
4
2
1
-
-
4
1
-
-
-
-
2
2
-
-
-
737150
Soni
Depletion of M. tuberculosis G ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618, Mycobacterium tuberculosis H37Rv
PLoS Pathog.
11
e1005235
2015
-
1
1
1
-
-
2
-
-
-
-
6
-
12
-
-
-
-
-
-
-
-
6
-
1
-
-
-
1
-
-
1
-
-
1
-
1
1
1
1
-
-
1
2
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
737291
Rani
High-throughput screen identif ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Tuberculosis
95
664-677
2015
-
-
1
-
-
-
6
3
-
1
-
4
-
11
-
-
1
-
-
-
-
-
5
-
1
-
-
-
1
-
-
1
5
-
10
-
-
1
1
-
-
-
10
8
5
5
-
1
-
4
-
-
-
1
-
-
-
-
5
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
735396
Vithani
GlmU (N-acetylglucosamine-1-ph ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
Acta Crystallogr. Sect. F
70
703-708
2014
-
-
1
1
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
736058
Mehra
Identification and optimizatio ...
Escherichia coli, Escherichia coli ATCC 25922
Eur. J. Med. Chem.
92
78-90
2014
-
-
-
-
-
-
12
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
-
-
2
-
-
-
1
-
-
-
2
14
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
719064
Green
Inhibitors of acetyltransferas ...
Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Streptococcus pneumoniae
Bioorg. Med. Chem. Lett.
22
1510-1519
2012
-
-
-
2
-
-
156
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
4
4
4
-
-
-
4
-
-
-
-
-
150
-
-
-
-
2
-
-
150
156
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
4
4
-
-
-
4
-
-
-
-
4
4
-
-
-
719070
Stokes
Inhibitors of the acetyltransf ...
Escherichia coli, Haemophilus influenzae, Streptococcus pneumoniae
Bioorg. Med. Chem. Lett.
22
7019-7023
2012
-
-
-
-
-
-
54
-
-
-
-
3
-
5
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
52
-
-
-
-
-
-
-
52
54
-
-
-
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719137
Rodriguez-Diaz
Metabolic engineering of Lacto ...
Lactobacillus casei
Biotechnol. Bioeng.
109
1704-1712
2012
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
719411
Min
Structure-based virtual screen ...
Xanthomonas oryzae
Eur. J. Med. Chem.
53
150-158
2012
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
719574
Zhou
Identification of amino acids ...
Mycobacterium tuberculosis
Glycoconj. J.
29
297-303
2012
-
-
1
-
10
-
-
14
-
-
1
1
-
3
-
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