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Information on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase
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EC Tree
2.3.1.157 glucosamine-1-phosphate N-acetyltransferaseIUBMB Comments
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.
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Word Map
- 2.3.1.157
- peptidoglycan
- utp
- drug development
- tokodaii
- glucosamine-6-phosphate
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left-hand
- udp-sugars
- glmm
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nucleotidylyltransferase
- utase
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diphosphate-n-acetylglucosamine
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
n-acetylglucosamine-1-phosphate uridyltransferase, st0452 protein, udp-glcnac pyrophosphorylase, glmu acetyltransferase, st0452, glmu enzyme, glucosamine-1-phosphate acetyltransferase, glmu uridyltransferase, glcnac-1-p uridyltransferase, glcn-1-p actase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional GlmU protein
bifunctional N-acetyltransferase/uridylyltransferase
bifunctional protein GlmU
bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
GlcN-1-P acetyltransferase
GlcN-1-P AcTase
GlcNAc-1-P uridyltransferase
GlmU
GlmU acetyltransferase
GlmU enzyme
GlmU uridyltransferase
glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
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glucosamine-1-phosphate acetyltransferase
glucosamine-1-phosphate acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
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MtGlmU
N-acetylglucosamine-1-phosphate uridyltransferase
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
Rv1018c
ST0452
ST0452 protein
STK_04520
UDP-GlcNAc pyrophosphorylase
UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
additional information
bifunctional N-acetyltransferase/uridylyltransferase
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bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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GlmU
bifunctional enzyme with glucosamine 1-phosphate acetyltransferase and N-acetylglucosamine 1-phosphate uridyltransferase activities
GlmU
bifunctional enzyme with glucosamine 1-phosphate acetyltransferase and N-acetylglucosamine 1-phosphate uridyltransferase activities
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GlmU
bifunctional enzyme with glucosamine 1-phosphate acetyltransferase and N-acetylglucosamine 1-phosphate uridyltransferase activities
GlmU
bifunctional enzyme, also to possess the activity of EC 2.3.1.23, glucosamine-1-phosphate N-acetyltransferase
GlmU
bifunctional enzyme, also to possess the activity of EC 2.3.1.23, glucosamine-1-phosphate N-acetyltransferase
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GlmU
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
glucosamine-1-phosphate acetyltransferase
bifuncional enzyme, also N-acetylglucosamine-1-phosphate uridyltransferase activity
glucosamine-1-phosphate acetyltransferase
bifuncional enzyme, also N-acetylglucosamine-1-phosphate uridyltransferase activity
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glucosamine-1-phosphate acetyltransferase
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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MtGlmU
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
MtGlmU
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
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N-acetylglucosamine-1-phosphate uridyltransferase
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
N-acetylglucosamine-1-phosphate uridyltransferase
bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
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N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase
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UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the 2-amino group of glucosamine-1-phosphate is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
also N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = UDP-N-acetyl-D-glucosamine + diphosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
both reactions of bifunctional GlmU follow Michaelis Menten ordered bi-bi mechanism involving an obligatory order of binding of substrates to the enzyme
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
substrate recognition, and catalytic mechanism for acetyltransfer involving His374, Asn397 and Ala391, overview
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the multifunctional enzyme from Sulfolobus tokodaii {7} is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the catalytic mechanism is a SN2, bimolecular nucleophilic substitution reaction, catalyzed by the C-terminal domain. His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding
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
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the multifunctional enzyme from Sulfolobus tokodaii {7} is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
also N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = UDP-N-acetyl-D-glucosamine + diphosphate
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acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase
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.
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CAS REGISTRY NUMBER
COMMENTARY
9023-06-7
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9031-91-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
n-propionyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
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?
propionyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
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?
succinyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-succinyl-alpha-D-glucosamine 1-phosphate
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?
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
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?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
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?
acetyl-CoA + alpha-D-galactosamine 1-phosphate
CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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r
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
uncommon mode of acetyl-CoA binding in GlmUMtb in the U conformation, which is distinct from the L conformation seen in the available non-mycobacterial GlmU structures. Higly conserved Trp460 is critical for acetyl-CoA binding
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme utilizes ternary complex formation to transfer an acetyl from acetyl-coenzyme A to glucosamine 1-phosphate to form N-acetylglucosamine 1-phosphate. Steady-state kinetic studies and equilibrium binding experiments indicate that GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
the enzyme utilizes ternary complex formation to transfer an acetyl from acetyl-coenzyme A to glucosamine 1-phosphate to form N-acetylglucosamine 1-phosphate. Steady-state kinetic studies and equilibrium binding experiments indicate that GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
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?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
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-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
no activity with alpha-D-glucosamine 6-phosphate. The multifunctional enzyme is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase)
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-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
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-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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-
-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine
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-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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-
-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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-
-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
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-
-
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?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in bacterial cell wall biosynthesis
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-
?
D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathway
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-
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D-glucosamine 1-phosphate + acetyl-CoA
N-acetyl-D-glucosamine 1-phosphate + CoA
a mechanism is proposed in which the activation energy of the double negatively charged phosphorane transition state is lowered by charge compensation of Mg2+ and the side-chain of Lys22
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N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
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N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
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glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
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N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetylglucosamine + ?
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glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis
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UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
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UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine 1-phosphate + UMP
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UDP-N-acetyl-d-glucosamine + diphosphate
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
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UDP-N-acetyl-d-glucosamine + diphosphate
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
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r
additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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GlmU also catalyzes the reaction of the N-acetylglucosamine-1-phosphate uridyltransferase, EC 2.7.7.23, catalyzing the synthesis of UDP-GlcNAc from GlcNAc-1-phosphate and UTP
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additional information
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GlmU is a bifunctional enzyme converting alpha-D-glucosamine 1-phosphate to N-acetyl-alpha-D-glucosamine 1-phosphate and then catalyzing the formation of UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate and uridine triphosphate
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additional information
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N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, a bifunctional enzyme that catalyzes two key reactions: acetyltransfer and uridyltransfer at two independent domains, overview
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additional information
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N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, a bifunctional enzyme that catalyzes two key reactions: acetyltransfer and uridyltransfer at two independent domains, overview
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additional information
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
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additional information
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
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additional information
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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additional information
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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additional information
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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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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additional information
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coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme. Substrate recognition and catalytic mechanism for acetyl transfer, overview
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additional information
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coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme. Substrate recognition and catalytic mechanism for acetyl transfer, overview
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additional information
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the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
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additional information
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the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
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additional information
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GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
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additional information
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GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
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additional information
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GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate
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additional information
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the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
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additional information
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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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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additional information
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the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
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additional information
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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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
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additional information
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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additional information
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes
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additional information
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the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity. The ST0452 protein can catalyze the acetylation of both GlcN-1-P and GalN-1-P, while GalN-1-P AcTase activity is not detected in bacterial enzymes