Isocitrate lyase family is a family of evolutionarily related proteins. Isocitrate lyase () is an enzyme that catalyzes the conversion of isocitrate to succinate and glyoxylate. This is the first step in the glyoxylate bypass, an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. A cysteine, a histidine and a glutamate or aspartate have been found to be important for the enzyme's catalytic activity. Only one cysteine residue is conserved between the sequences of the fungal, plant and bacterial enzymes; it is located in the middle of a conserved hexapeptide. Other enzymes also belong to this family including carboxyvinyl-carboxyphosphonate phosphorylmutase () which catalyses the conversion of 1-carboxyvinyl carboxyphosphonate to 3-(hydrohydroxyphosphoryl) pyruvate carbon dioxide, and phosphoenolpyruvate mutase (), which is involved in the biosynthesis of phosphinothricin tripeptide antibiotics.

Subfamilies

Isocitrate lyase Isocitrate lyase (), or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle (T ...

Methylisocitrate lyase The enzyme methylisocitrate lyase () catalyzes the chemical reaction :(2''S'',3''R'')-3-hydroxybutane-1,2,3-tricarboxylate \rightleftharpoons pyruvate + succinate The reaction is similar to that of isocitrate lyase, except that an additional ...

Carboxyvinyl-carboxyphosphonate phosphorylmutase In enzymology, a carboxyvinyl-carboxyphosphonate phosphorylmutase () is an enzyme that catalyzes the chemical reaction :1-carboxyvinyl carboxyphosphonate \rightleftharpoons 3-(hydrohydroxyphosphoryl)pyruvate + CO2 Hence, this enzyme has one subs ...

References

Protein domains Protein families {{protein-stub