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Literature summary for 2.7.7.23 extracted from

  • 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 (2001), J. Biol. Chem., 276, 3833-3839.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
truncated and full length enzyme overexpressed in Escherichia coli, His-tag inserted for purification Escherichia coli

Protein Variants

Protein Variants Comment Organism
DELTA1-130 deletion of N-terminus, very low activity Escherichia coli
DELTA1-182 deletion of N-terminus, very low activity Escherichia coli
DELTA1-227 deletion of N-terminus, very low activity Escherichia coli
DELTA1-233 deletion of N-terminus, very low activity Escherichia coli
DELTA1-250 deletion of N-terminus Escherichia coli
DELTA1-26 deletion of N-terminus Escherichia coli
DELTA1-78 deletion of N-terminus, very low activity Escherichia coli
DELTA227-456 deletion of C-terminus Escherichia coli
DELTA250-456 deletion of C-terminus, low activity Escherichia coli
DELTA331-456 deletion of C-terminus, roughly 50% of activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24700
-
SDS-PAGE, enzyme variant del233 Escherichia coli
25600
-
SDS-PAGE, enzyme variant del227 Escherichia coli
28600
-
SDS-PAGE, enzyme variant Tr250 Escherichia coli
36200
-
SDS-PAGE, enzyme variant del130 Escherichia coli
37100
-
SDS-PAGE, Tr331 Escherichia coli
41800
-
SDS-PAGE, enzyme variant del78 Escherichia coli
50100
-
SDS-PAGE, calculated from DNA sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + UDP-N-acetyl-D-glucosamine Escherichia coli amino sugar metabolism UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
diphosphate + UDP-N-acetyl-D-glucosamine Escherichia coli JM83 amino sugar metabolism UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
full length and truncated enzymes using His-tag Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + UDP-N-acetyl-D-glucosamine
-
Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
-
Escherichia coli JM83 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Escherichia coli JM83 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r

Subunits

Subunits Comment Organism
trimer 3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer) Escherichia coli

Synonyms

Synonyms Comment Organism
More bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
N-acetyl-D-glucosamine 1-phosphate purified del227 enzyme, pH 7.4 Escherichia coli
0.2
-
N-acetyl-D-glucosamine 1-phosphate purified del233 enzyme, pH 7.4 Escherichia coli
0.25
-
N-acetyl-D-glucosamine 1-phosphate purified del78 enzyme, pH 7.4 Escherichia coli
0.35
-
N-acetyl-D-glucosamine 1-phosphate purified del130 enzyme, pH 7.4 Escherichia coli
8
-
N-acetyl-D-glucosamine 1-phosphate purified Tr250 enzyme, pH 7.4 Escherichia coli
140
-
N-acetyl-D-glucosamine 1-phosphate purified Tr331 enzyme, pH 7.4 Escherichia coli
330
-
N-acetyl-D-glucosamine 1-phosphate purified full length enzyme, pH 7.4 Escherichia coli