EC Number |
General Information |
Reference |
---|
4.2.1.36 | evolution |
the mutations of the small-subunit HACN protein MJ1271 loop-region may reverse the evolution of HACN activity from an ancestral IPMI gene, demonstrating the evolutionary potential for promiscuity in hydro-lyase enzymes. Understanding these specificity determinants enables the functional reannotation of paralogous HACN and isopropylmalate isomerase, IPMI, genes in numerous genome sequences |
702368 |
4.2.1.36 | malfunction |
deletion of the LYS4 gene results in lysine auxotrophy. The mutant shows increased sensitivity to oxidative stress, agents that challenge cell wall/membrane integrity, and azole antifungal drugs |
746978 |
4.2.1.36 | malfunction |
L2 mutant is deficient in homoaconitase activity since it is complemented by the Aspergillus nidulans lysF gene. Wis 54-1255 gene lys3 complements the L2 mutation. Accumulation of homocitric acid in the L2 strain, resulting from the mutation in the lys3 (homoaconitase) gene, is required for the upregulation of the lysine biosynthetic genes. The mutant Lys3 protein is altered in a region required to bind the [4Fe-4S] cluster |
705575 |
4.2.1.36 | metabolism |
the enzyme is involved in the lysine biosynthetic pathway |
746978 |
4.2.1.36 | more |
the enzymes' stereospecific hydrolyase activity make it an attractive catalyst to produce diastereomers from unsaturated precursors |
702368 |
4.2.1.36 | physiological function |
homoaconitase proteins catalyze the isomerization of tricarboxylates with variable chain length gamma-carboxylate groups |
702368 |
4.2.1.36 | physiological function |
Lys4 plays an important role in mitochondrial iron metabolism, and is required for proper mitochondrial function in Cryptococcus neoformans. LYS4 is required for full virulence in Cryptococcus neoformans |
746978 |
4.2.1.36 | physiological function |
lysF gene can complement the Penicillium chrysogenum L2 mutant deficient in homoaconitase activity |
705575 |