2.7.7.33: glucose-1-phosphate cytidylyltransferase

This is an abbreviated version!
For detailed information about glucose-1-phosphate cytidylyltransferase, go to the full flat file.

Reaction

Synonyms

alpha-D-glucose-1-phosphate cytidylyltransferase, CDP-D-glucose synthase, CDP-glucose pyrophosphorylase, CDPglucose pyrophosphorylase, cytidine diphosphate glucose pyrophosphorylase, cytidine diphosphate-D-glucose pyrophosphorylase, cytidine diphosphoglucose pyrophosphorylase, cytidylyltransferase, glucose 1-phosphate

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.7 Nucleotidyltransferases

                2.7.7.33 glucose-1-phosphate cytidylyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	Activating Compound
3805	AA Sequence
1	Application
1	CAS Registry Number
5	Cloned(Commentary)
2	Crystallization (Commentary)
2	General Stability
25	Inhibitors
3	Ki Value [mM]
27	KM Value [mM]
21	Metals/Ions
7	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
13	Organism
7	Pathway
2	PDB ID
6	pH Optimum
1	pH Range
2	pH Stability
3	Purification (Commentary)
1	Reaction
2	Reaction Type
12	Reference
5	Specific Activity [micromol/min/mg]
5	Storage Stability
43	Substrates and Products (Substrate)
3	Subunits
12	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]

Crystallization

print visible entries

print all entries

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

Crystallization on EC 2.7.7.33 - glucose-1-phosphate cytidylyltransferase

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

top print hide Go to Crystallization (commentary) Search

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

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging-drop vapour-diffusion method, crystallized in the presence of its product, CDP-glucose. Enzyme exists as a fully integrated hexamer with 32-point group symmetry

Salmonella enterica subsp. enterica serovar Typhi

-

662281

hanging-drop vapour-diffusion method.The structure of the enzyme with bound MgCTP reveals that the binding pocket for the nucleotide is contained within one subunit rather than shared between two. Key side chains involved in nucleotide binding include Thr14, Arg15, Lys25, and Arg111

Salmonella enterica subsp. enterica serovar Typhi

-

662329