MAOC Leishmania

The Maoc Family Dehydratase-Like Protein is part of a conserved protein domain family known as MaoC_dehydratas . This family includes enzymes that share structural similarities with a variety of other enzymes, such as estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, and the fatty acid synthase beta subunit . The MaoC gene is typically part of an operon with maoA, which is involved in the synthesis of monoamine oxidase .

MaoC proteins are known for their ®-specific enoyl-CoA hydratase activity . This activity is crucial in various metabolic pathways, including fatty acid metabolism and the synthesis of monoamine oxidase . The protein is found in a wide range of organisms, from bacteria to humans .

The expression of MaoC-like proteins can vary significantly between different organisms and tissues. For example, in a study involving the expression of His-tagged MaoC in E. coli, the protein comprised about 40% of the total protein and was largely soluble . This high level of expression did not affect cell growth, indicating that the protein can be expressed efficiently without detrimental effects on the host organism .

MaoC-like proteins play a crucial role in various metabolic pathways. They are involved in the hydration of enoyl-CoA derivatives, which is a key step in fatty acid metabolism . This activity is essential for the proper functioning of cellular metabolism and energy production .

The MaoC-like proteins function by catalyzing the hydration of enoyl-CoA derivatives, converting them into 3-hydroxyacyl-CoA . This reaction is a critical step in the beta-oxidation of fatty acids, which is a major pathway for energy production in cells .

The regulation of MaoC-like proteins can occur at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications . For instance, in the context of Leishmania donovani, the Maoc family dehydratase-like protein was found to be differentially modulated during the promastigote to amastigote differentiation . This suggests that the protein’s expression and activity can be tightly regulated in response to specific cellular conditions and developmental stages .