Jump to Main Content
- Federico, Rodolfo, et al. Show all 10 Authors
- Amino acids 2016 v.48 no.10 pp. 2283-2291
- X-ray diffraction; blood serum; cattle; crystal structure; cysteine; denaturation; differential scanning calorimetry; disulfide bonds; enzyme activity; fluorescence emission spectroscopy; gel electrophoresis; gels; hydrogen peroxide; mutants; spermidine; spermine; staining; thermal stability; yeasts
- ... Spermine oxidase (SMOX) is a flavin-containing enzyme that specifically oxidizes spermine to produce spermidine, 3-aminopropanaldehyde and hydrogen peroxide. While no crystal structure is available for any mammalian SMOX, X-ray crystallography showed that the yeast Fms1 polyamine oxidase has a dimeric structure. Based on this scenario, we have investigated the quaternary structure of the SMOX prot ...
- Federico, Rodolfo, et al. Show all 8 Authors
- Amino acids 2011 v.40 no.4 pp. 1115-1126
- active sites; biosynthesis; catalytic activity; cell growth; enzyme substrates; enzymes; mammals; molecular models; neoplasms; site-directed mutagenesis; spermine; structure-activity relationships; substrate specificity; yeasts
- ... Spermine oxidase (SMO) and acetylpolyamine oxidase (APAO) are FAD-dependent enzymes that are involved in the highly regulated pathways of polyamine biosynthesis and degradation. Polyamine content is strictly related to cell growth, and dysfunctions in polyamine metabolism have been linked with cancer. Specific inhibitors of SMO and APAO would allow analyzing the precise role of these enzymes in po ...