Literature summary extracted from
Moche, M.; Dehesh, K.; Edwards, P.; Lindqvist, Y.
The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54.ANG. resolution and its relationship to other condensing enzymes (2001), J. Mol. Biol., 305, 491-503.
Application
EC Number |
Application |
Comment |
Organism |
---|
2.3.1.41 |
medicine |
target for the development of drugs for the treatment of cancer and tuberculosis |
Synechocystis sp. |
2.3.1.41 |
nutrition |
target for the engineering of plant seed oils |
Synechocystis sp. |
2.3.1.41 |
pharmacology |
target for the development of drugs for the treatment of cancer and tuberculosis, involved in biosynthesis of precursors of pharmacological agents |
Synechocystis sp. |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.3.1.41 |
expression in Escherichia coli |
Synechocystis sp. |
2.3.1.179 |
expression in Escherichia coli |
Synechocystis sp. |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.3.1.41 |
hanging drop vapour diffusion method, protein solution: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 75 mM imidazole, reservoir solution: 0.085 M tri-sodium citrate, 0.17 M ammonium acetate, 22% w/v polyethylene glycol 4000, 15% v/v glycerol as cryo-protectant, 15% w/v 1,2,3-heptanetriol, x-ray structure analysis, three-dimensional model |
Synechocystis sp. |
2.3.1.179 |
rod-shaped crystals of the purified enzyme are grown in two weeks by the hanging-drop vapor-diffusion method, 1.54 A resolution, space group P3(1)21, cells dimensions: a = b = 100.8 A, c = 74.7 A |
Synechocystis sp. |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.3.1.41 |
Synechocystis sp. |
- |
isozyme II |
- |
2.3.1.179 |
Synechocystis sp. |
P73283 |
PCC 6803 |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.3.1.41 |
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] |
structure of active site, substrate binding pocket, and subunit structure in relation to substrate specificity of the 3 isozyme types |
Synechocystis sp. |
|
2.3.1.41 |
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] |
active site cysteine |
Synechocystis sp. |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.3.1.41 |
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] |
- |
Synechocystis sp. |
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein] |
- |
r |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.3.1.41 |
dimer |
crystal structure analysis of subunits |
Synechocystis sp. |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.3.1.41 |
KAS |
- |
Synechocystis sp. |
2.3.1.41 |
More |
3 structural classes of condensing enzymes |
Synechocystis sp. |