2.7.7.23: UDP-N-acetylglucosamine diphosphorylase

This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine diphosphorylase, go to the full flat file.

Reaction

Synonyms

acetylglucosamine 1-phosphate uridylyltransferase, AGX-1, AGX1, AGX2, amino-sugar-1-phosphate acetyltransferase, bifunctional N-acetyltransferase/uridylyltransferase, BmUAP, CL6EHI_021200, CL6EHI_039830, EcGlmU, EnhiA.01126.a, EnhiA.01126.b, GlcNAc-1-P uridyltransferase, GlcNAc-1-P UTase, GlcNAc-1-phosphate nucleotidylyltransferase, GLCNAC1PUT1, GLCNAC1PUT2, GlmU, GlmUMTB, hiGlmU, LmUAP1, LmUAP2, LOC_Os08g10600, Mmy, More, mummy, N-acetyl-D-glucosamine-1-phosphate uridylyltransferase, N-acetyl-glucosamine-1-phosphate uridyltransferase, N-acetylglucosamine 1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate uridyltransferase, N-acetylglucosamine-1-phosphate uridylyltransferase, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase, Os08g10600, Rv1018c, spl29, spotted leaf 29, ST0452, ST0452 protein, STK_04520, Tb11.02.0120, UAP, UAP enzyme, UAP1, UAP2, UDP N-acetylglucosamine pyrophosphorylases 1, UDP N-acetylglucosamine pyrophosphorylases 2, UDP-GlcNAc pyrophosphorylase, UDP-GlcNAc pyrophosphorylase (UAP), UDP-HexNAc pyrophosphorylase, UDP-N-acetylgalactosamine pyrophosphorylase, UDP-N-acetylglucosamine diphosphorylase 1, UDP-N-acetylglucosamine diphosphorylase 2, UDP-N-acetylglucosamine pyrophosphorylase, UDP-N-acetylglucosamine pyrophosphorylase (UAP), UDP-N-acetylglucosamine pyrophosphorylase 1, UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase, UDP-N-acetylglucosamine-diphosphorylase, UDP-N-acetylhexosamine pyrophosphorylase, UDPacetylglucosamine pyrophosphorylase, UNAcP, uridine diphosphate N-acetylglucosamine pyrophosphorylase, uridine diphosphate-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, uridine diphosphoacetylglucosamine pyrophosphorylase, uridine-diphospho-N-acetylglucosamine pyrophosphorylase, UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase, UTP:N-acetylglucosamine-1-P uridylyltransferase, Ydl103c protein

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.7 Nucleotidyltransferases

                2.7.7.23 UDP-N-acetylglucosamine diphosphorylase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
8	Activating Compound
29531	AA Sequence
17	Application
1	CAS Registry Number
49	Cloned(Commentary)
2	Cofactor
22	Crystallization (Commentary)
35	Disease/ Diagnostics
11	Expression
98	General Information
8	General Stability
55	IC50 Value
146	Inhibitors
30	kcat/KM [mM/s]
7	Ki Value [mM]
76	KM Value [mM]
7	Localization
77	Metals/Ions
36	Molecular Weight [Da]
139	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
477	Organism
9	Pathway
84	PDB ID
40	pH Optimum
5	pH Range
2	pH Stability
4	pI Value
1	Posttranslational Modification
247	Protein Variants
48	Purification (Commentary)
2	Reaction
1	Reaction Type
126	Reference
60	Source Tissue
73	Specific Activity [micromol/min/mg]
15	Storage Stability
258	Substrates and Products (Substrate)
38	Subunits
215	Synonyms
1	Systematic Name
30	Temperature Optimum [°C]
3	Temperature Range [°C]
5	Temperature Stability [°C]
42	Turnover Number [1/s]

Posttranslational Modification

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Posttranslational Modification on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Posttranslational Modification Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

phosphoprotein

Mycobacterium tuberculosis

P9WMN3

the enzyme is regulated by PknB via phosphorylation at Thr418 causing downregulation of acetyltransferase activity leaving its uridyltransferase activity unaffected, identification of phosphorylation site by mass spectrometry

720042