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L-cysteine:molybdenum cofactor sulfurtransferase
Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 220.127.116.11), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.
the enzyme is involved in aldehyde oxidase activity in Arabidopsis, which indirectly regulates absisic acid biosynthesis and increases stress tolerance. Overexpression of the enzyme prevents water loss and modulates stomatal closure, enhances expression of stress-upregulated genes and promotes absisic acid accumulation to drought stress. Enzyme overexpression also enhances biomass accumulation and produces higher yield in the field
enzyme overexpression in transgenic tobacco can enhance drought tolerance. Enzyme overexpressing tobacco seedlings show lower transpirational water loss than that of nontransgenic seedlings in the same period under normal conditions. Transgenic plants show less wilting, maintain higher water content and better cellular membrane integrity, accumulate higher quantities of abscisic acid and proline, and exhibit higher activities of antioxidant enzymes, i.e., superoxide dismutase, catalase, peroxidase and ascorbate peroxidase, as compared with control plants
overexpression of Arabidopsis molybdenum cofactor sulfurase gene LOS5 in maize markedly enhances the expression and activity of aldehyde oxidase, leading to absisic acid accumulation and increased drought tolerance by decreasing stomatal aperture to reduce water loss. LOS5 overexpression enhances abiotic stress-related genes