 |
 |
The tridimensional structure of this enzyme has not been resolved yet.
a-IPM synthetase
1.Carbon-carbon lyases
3.Oxo-acid-lyases
acetyl-CoA
+ 3-methyl-2-oxobutanoate + H2OCoA
3-methyl-2-oxobutanoate
H2O
The following enzymes have been shown to be functionally as well as evolutionary related:
-a-isopropylmalate synthase which catalyzes the first step in the biosynthesis of leucine, the condensation of acetyl-CoA and a-ketoisovalerate to form 2-isopropylmalate synthase.
--Homocitrate synthase (EC 4.1.3.21) which is involved in the biosynthesis of the iron-molybdenum cofactor of nitrogenase and catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate into homocitrate.
Two conserved regions has been selected as signature patterns for these
enzymes. The first region is located in the N-terminal section while the
second region is located in the central section and contains two conserved
histidine residues which could be implicated in the catalytic mechanism.
Reference