2.3.1.29: glycine C-acetyltransferase

This is an abbreviated version!
For detailed information about glycine C-acetyltransferase, go to the full flat file.

Reaction

Synonyms

2-amino-3-ketobutyrate CoA ligase, 2-amino-3-ketobutyrate coenzyme A ligase, 2-amino-3-ketobutyrate-CoA ligase, 2-amino-3-oxobutyrate CoA ligase, acetyltransferase, glycine, alpha-amino-beta-oxobutyrate CoA-ligase, aminoacetone synthase, aminoacetone synthetase, glycine acetyltransferase, KBL

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.29 glycine C-acetyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
5	Activating Compound
13831	AA Sequence
2	Application
1	CAS Registry Number
10	Cloned(Commentary)
12	Cofactor
1	Crystallization (Commentary)
1	General Information
5	General Stability
34	Inhibitors
2	Ki Value [mM]
10	KM Value [mM]
9	Localization
21	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
119	Organism
5	Pathway
28	PDB ID
6	pH Optimum
2	pH Range
1	pH Stability
2	Posttranslational Modification
7	Purification (Commentary)
5	Reaction
1	Reaction Type
19	Reference
9	Source Tissue
5	Specific Activity [micromol/min/mg]
41	Substrates and Products (Substrate)
10	Subunits
15	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Stability [°C]

Crystallization

print visible entries

print all entries

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

Crystallization on EC 2.3.1.29 - glycine C-acetyltransferase

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

external aldimine in the crystal structure, interaction between aldimine and the side chains in the substrate binding site explain the specificity to the substrate

Escherichia coli

P0AB77

486747