By Esmond E. Snell (auth.), G. Marino, G. Sannia, F. Bossa (eds.)

The Intemational assembly on diet B6 and Carbonyl Catalysis happened on Capri, Italy from twenty second to twenty seventh might 1994 and used to be geared up along with the third Symposium on PQQ and Quinoproteins. It used to be a unprecedented social gathering for scientists from around the world to satisfy and speak about new advancements in those overlapping fields. a number of classes have been devoted to the molecular features of nutrition B6 and Quinone established enzymes, in addition to to the mobile, biomedical and dietary facets. The congress was once inaugurated by means of Paolo Fasella in his potential as normal Director of technology, examine and improvement of the fee of the ecu groups, with an outline on Intemational medical Collaboration. The clinical periods begun with a conversation at the heritage of nutrition B6 given via David Metzler who on the final minute awarded Esmond Snell's paper including a few own feedback. regrettably, either Esmond Snell and Alton Meister needed to all at once cancel the journey to Capri. those complaints include the papers provided as oral contributions and some chosen poster shows. The restricted variety of pages intended shall we now not post many fascinating poster shows, together with these chosen for the 3 full of life and fascinating night poster dialogue periods referred to as through the organizers "Vino, taralli and ... discussion".

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Bossa F. and Schirch V. (1993). Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase. 1. Bioi. Chem. 268: 23132-23138. Thorson J. , Lo S. , Liu H-w. and Hutchinson C. R. (1993). Biosynthesis of 3,6-didehoxyexoses: new mechanistic reflections upon 2,6·dideoxy, 4,6-dideoxy, and amino sugar construction. 1. Am. Chem Soc. 115: 6993-6994. Toney M. , Cowan S. W. and Jansonius J. N. (1993). Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites.

The alignment (Fig. , 1994), Asp222, Lys258, and Arg386 according to the AAT numbering system. The SHMT predicted secondary structure generally agrees with the experimentally observed structures for the three enzymes. Also, the alignment matches 80% of the core residues buried in all three structures (fractional side chain accessibility less than 5%) with conserved hydrophobic side chains in the 14 Table I. G MLLILDEAQTGV AYLFVDMAHVAG AYLFADIAHIAG AYLFVDMAHVAG AYLMVDMAHIAG AIFLVDMAHFAG AYLLVDMAHFAG AYLVVDMAHISG AYLMADMAHISG AYLMADMAHISG AYLMADMAHISG AHLLADMAHISG AHLLADMAHISG AVLLADMAHISG AYLFVDMAHVAG 258 DGCTMSGKKDCLV VVLSQSYAKNMGL DI LTLS ..

SCruttllll, N. , Hinchliffe, N. , Perham, R. , and Cerami, A. (1991) Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction. Proc. Natl. Acad. Sci. 88: 8769-8773. 1ulin, D. , and Kirsch, 1. F. (1989) Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism. Biochemistry 28: 3825-3833. Kiick, D. M. and Cook, P. F. (1983) pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase.

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