Francesco De Lorenzo

Last updated
Francesco De Lorenzo
Francesco De Lorenzo.jpg
Minister of Health
In office
22 July 1989 21 February 1993
Occupation Politician

Francesco De Lorenzo (born June 5, 1938 in Naples) is an Italian physician and politician and is a member of the Italian Liberal Party.

Contents

Life and Works

He was born in Naples on June 5, 1938. He was minister of health (1989–1993) in the Government of Italy. He served in the cabinet of Prime Minister Bettino Craxi (1986–1987), Giulio Andreotti (1989–1992) and Giuliano Amato (1992–1993). He also served in the Chamber of Deputies of Italy in Legislature IX (1983–1987), Legislature X (1987–1992) and Legislature XI (1992–1994).

He was a central figure in the Tangentopoli bribery scandal uncovered by the Mani pulite investigations of the early 1990s.

Publications

Related Research Articles

<span class="mw-page-title-main">Ames test</span> Biological testing method

The Ames test is a widely employed method that uses bacteria to test whether a given chemical can cause mutations in the DNA of the test organism. More formally, it is a biological assay to assess the mutagenic potential of chemical compounds. A positive test indicates that the chemical is mutagenic and therefore may act as a carcinogen, because cancer is often linked to mutation. The test serves as a quick and convenient assay to estimate the carcinogenic potential of a compound because standard carcinogen assays on mice and rats are time-consuming and expensive. However, false-positives and false-negatives are known.

<span class="mw-page-title-main">Auxotrophy</span> Inability to synthesize an organic compound required for growth

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<span class="mw-page-title-main">Catalytic triad</span> Set of three coordinated amino acids

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<span class="mw-page-title-main">Micrococcal nuclease</span> Class of enzymes

Micrococcal nuclease is an endo-exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'-phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved.

<span class="mw-page-title-main">Bovine pancreatic ribonuclease</span>

Bovine pancreatic ribonuclease, also often referred to as bovine pancreatic ribonuclease A or simply RNase A, is a pancreatic ribonuclease enzyme that cleaves single-stranded RNA. Bovine pancreatic ribonuclease is one of the classic model systems of protein science. Two Nobel Prizes in Chemistry have been awarded in recognition of work on bovine pancreatic ribonuclease: in 1972, the Prize was awarded to Christian Anfinsen for his work on protein folding and to Stanford Moore and William Stein for their work on the relationship between the protein's structure and its chemical mechanism; in 1984, the Prize was awarded to Robert Bruce Merrifield for development of chemical synthesis of proteins.

<span class="mw-page-title-main">Histidinol dehydrogenase</span>

In enzymology, histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction

Alkylglycerol monooxygenase (AGMO) is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipids. This enzyme was first described in 1964 as a pteridine-dependent ether lipid cleaving enzyme. In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7. In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.

Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a protein-disulfide reductase (glutathione) is an enzyme that catalyzes the chemical reaction

The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction

The enzyme dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) catalyzes the chemical reaction

<span class="mw-page-title-main">Imidazoleglycerol-phosphate dehydratase</span>

The enzyme imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) catalyzes the chemical reaction

In enzymology, a polar-amino-acid-transporting ATPase (EC 3.6.3.21) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction

In enzymology, a glycerophospholipid acyltransferase (CoA-dependent) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase</span> Class of enzymes

In enzymology, a nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Hydroxyethylthiazole kinase</span>

In enzymology, a hydroxyethylthiazole kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a protein-histidine tele-kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cob(I)yrinic acid a,c-diamide adenosyltransferase</span> Class of enzymes

In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.

In enzymology, a ceramide phosphoethanolamine synthase is an enzyme that catalyzes the chemical reaction

References

    Preceded by Minister of Health of Italy
    1989–1993
    Succeeded by