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See detailStructure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution.
Dideberg, O.; Charlier, Paulette ULg; Dive, Georges ULg et al

in Nature (1982), 299(5882), 469-470

Bacteria possess proteases that are specific for the peptide bonds between D-alanine residues, one of which has a free alpha-carboxyl group. These D-alanyl-D-alanine peptidases catalyse carboxypeptidation ... [more ▼]

Bacteria possess proteases that are specific for the peptide bonds between D-alanine residues, one of which has a free alpha-carboxyl group. These D-alanyl-D-alanine peptidases catalyse carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism1,2, and are inactivated by beta-lactam antibiotics. We have now elucidated the structure, at 2.5 Å resolution, of the penicillin-resistant Zn2+-containing D-alanyl-D-alanine peptidase of Streptomyces albus (Zn2+ G peptidase)3,4. The enzyme is shown to consist of two globular domains, connected by a single link. The N-terminal domain has three alpha-helices, and the C-terminal domain has three alpha-helices and five beta-strands. The Zn2+ ion is ligated by three histidine residues, and located in a cleft in the C-terminal domain. The mechanism of action of the enzyme may be related to that of other carboxypeptidases, which also contain functional Zn2+ ions. [less ▲]

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See detailDexamethasone-induced accumulation of a fibronectin and collagen extracellular matrix in transformed human cells.
Furcht, L. T.; Mosher, D. F.; Wendelschafer-Crabb, G. et al

in Nature (1979), 277(5695), 393-5

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See detailSynthesis of growth hormone by bacteria
Seeburg, P. H.; Shine, J.; Martial, Joseph ULg et al

in Nature (1978), 276(5690), 795-8

A hybrid gene was constructed between the beta-lactamase gene of plasmid pBR322 and the cloned coding sequence for rat growth hormone. This gene is expressed in bacteria and growth hormone sequences are ... [more ▼]

A hybrid gene was constructed between the beta-lactamase gene of plasmid pBR322 and the cloned coding sequence for rat growth hormone. This gene is expressed in bacteria and growth hormone sequences are detectable by immunological methods. [less ▲]

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See detailNucleotide sequence and amplification in bacteria of structural gene for rat growth hormone
Seeburg, P. H.; Shine, J.; Martial, Joseph ULg et al

in Nature (1977), 270(5637), 486-94

The primary structure of DNA containing the sequence for rat pituitary growth hormone mRNA has been determined. DNA was obtained by reverse transcription of polyadenylated RNA from cultured pituitary ... [more ▼]

The primary structure of DNA containing the sequence for rat pituitary growth hormone mRNA has been determined. DNA was obtained by reverse transcription of polyadenylated RNA from cultured pituitary cells and from recombinant bacterial plasmids. The amino acid sequences for rat growth hormone and its precursor form have been deduced from the determined nucleotide sequences. [less ▲]

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See detailConstruction and analysis of recombinant DNA for human chorionic somatomammotropin
Shine, J.; Seeburg, P. H.; Martial, Joseph ULg et al

in Nature (1977), 270(5637), 494-499

DNA complementary to mRNA coding for the human polypeptide hormone, chorionic somatomammotropin, has been purified by specific restriction endonuclease digestion and religation before cloning into ... [more ▼]

DNA complementary to mRNA coding for the human polypeptide hormone, chorionic somatomammotropin, has been purified by specific restriction endonuclease digestion and religation before cloning into bacterial plasmids. The primary structure of a major portion of this mRNA species is deduced from the nucleotide sequence of the recombinant DNA. [less ▲]

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See detailFate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61
Frère, Jean-Marie ULg; Ghuysen, Jean-Marie ULg; Vanderhaeghe, Hubert et al

in Nature (1976), 260(5550), 451-454

LIKE various beta-lactamases, acylases and esterases1, the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61 degrades benzylpenicillin and other beta-lactam antibiotics2-4. The R61 enzyme ... [more ▼]

LIKE various beta-lactamases, acylases and esterases1, the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61 degrades benzylpenicillin and other beta-lactam antibiotics2-4. The R61 enzyme, however, markedly differs from the other penicillin-degrading enzymes in causing fragmentation of the penicillin nucleus. By using 8-14C-benzylpenicillin (benzyl labelled) as substrate, one of the fragments produced was shown to be 14C-phenylacetylglycine5. The reaction with the R61 enzyme is also peculiar in that it is a slow process. This is because of the long half life of the stoichiometnc complex transitorily formed between the antibiotic and the enzyme. Thus, for example, the value of the half life for the complex formed with benzylpenicillin is 80 min in 10 mM phosphate buffer (pH 7.0) and at 37 °C. As breakdown of the complex proceeds, however, phenylacetylglycine (when benzylpenicillin is used as substrate) is released and the enzyme concomitantly recovers its ability to bind penicillin. We have now characterised the fragment (hereby designated as the Y product) arising from the thiazolidine ring of penicillin as a result of the fragmentation of the antibiotic molecule by the R61 enzyme. [less ▲]

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See detailDiffusion of copper in the animal kingdom
Fredericq, Léon ULg

in Nature (1880), XXXI

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