3-(imidazol-5-yl)lactate dehydrogenase

3-(imidazol-5-yl)lactate dehydrogenase (I5LDH) is a hypothetical enzyme that, based on its name, would likely catalyze the reversible interconversion of 3-(imidazol-5-yl)lactate and a corresponding keto form, using either NAD+ or NADP+ as a cofactor. It is presumed to function as a dehydrogenase, similar to other lactate dehydrogenases, facilitating the transfer of a hydride ion and a proton between the substrate and the cofactor.

Given the "3-(imidazol-5-yl)" moiety attached to the lactate structure, this enzyme's activity would be related to a compound incorporating an imidazole ring, a structural feature common in histidine. Therefore, I5LDH could be involved in a metabolic pathway concerning modified histidine or imidazole-containing compounds.

Currently, there is limited documented scientific literature readily available explicitly describing a well-characterized enzyme with this precise name and function. The name appears to be derived from chemical nomenclature principles implying the possible substrate specificity, rather than representing a thoroughly researched and characterized enzyme in existing biological systems. If such an enzyme exists, its specific biological role, kinetic parameters, and regulatory mechanisms would require further experimental investigation and publication. It is possible that the enzyme is part of a theoretical metabolic pathway, or that its function has been described under a different, more common name.