Crystallization (Comment) | Organism |
---|---|
purified FabH as apoenzyme or ligand-bound complex, X-ray diffraction structure determination and analysis at 1.46 A resolution | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | the enzyme is important in fatty acid biosynthesis | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6R0 | gene fabH | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | catalytic reaction mechanism might include a water molecule or a hydroxyl anion in Cys112 deprotonation, large conformational changes in the active site e.g. through disordering of four essential loops and the movement of the two catalytic residues Cys112 and His244 | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is important in fatty acid biosynthesis | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | three-dimensional structure analysis, the enzyme contains a large solvent-accessible channel in the dimer interface as well as two cis-peptides, cis-Pro88 and cis-Phe308, in two of the disordered loops, structural instability | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
beta-ketoacyl-acyl carrier protein synthase III | - |
Escherichia coli |
FabH | - |
Escherichia coli |