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

ISBN-10: 303487393X

ISBN-13: 9783034873932

ISBN-10: 3034873956

ISBN-13: 9783034873956

The Intemational assembly on diet B6 and Carbonyl Catalysis came about on Capri, Italy from twenty second to twenty seventh could 1994 and used to be geared up along with the third Symposium on PQQ and Quinoproteins. It was once a unprecedented celebration for scientists from worldwide to fulfill and speak about new advancements in those overlapping fields. numerous classes have been devoted to the molecular facets of diet B6 and Quinone based enzymes, in addition to to the mobile, biomedical and dietary features. The congress used to be inaugurated via Paolo Fasella in his potential as basic Director of technological know-how, study and improvement of the fee of the eu groups, with an outline on Intemational medical Collaboration. The medical periods all started with a conversation at the background of nutrition B6 given through David Metzler who on the final minute awarded Esmond Snell's paper including a few own comments. regrettably, either Esmond Snell and Alton Meister needed to abruptly cancel the journey to Capri. those lawsuits comprise the papers awarded as oral contributions and some chosen poster shows. The constrained variety of pages intended shall we now not post many attention-grabbing poster displays, together with these chosen for the 3 full of life and interesting night poster dialogue classes referred to as through the organizers "Vino, taralli and ... discussion".

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Was supported in part by NIH Molecular Biophysics Training Grant GM-08295. , Biicheler, U. , and Walsh, C. T. (1991) Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase. Biochemistry 30: 6124-6127. Dunn, C. , Wilks, H. , Halsall, D. , Clarke, A. , and Holbrook, 1. 1. (1991) Design and synthesis of new enzymes based on the lactate dehydrogenase framework. Phil. Trans. R. Soc. Lond. B 332: 177-184. Estell, D. , Graycar, T. , Miller, 1. , Powers, D. , Bumier, 1.

Sequence alignments of eT ATase and eAATase show ca. 43% sequence identity and 72% similarity; therefore both enzymes must share close secondary and tertiary structure. Six active site residues of eAATase were targeted by homology modeling as likely determinants of aromatic amino acid reactivity with eTATase. Two of these (Thrl09 and Asn297) are invariant in all known aspartate aminotransferase enzymes, but differ in eTATase (Serl09 and Ser297). The other four (VaI39, Lys41, Thr47, and Asn69) line the active site pocket of eAATase, and are replaced by amino acids with more nonpolar side chains in eTATase (Leu39, Tyr41, Ile47, and Leu69).

Mol. Bioi. 227: 197-213. 1. and Christen, P. (1993) Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. I. Biochem. 214: 549-561. , Kaiser-Kupfer, M. and Valle, D. (1989) At least two mutant alleles of ornithine &-aminotransferase cause gyrate atrophy of the choroid and retina in Finns. Proc. Natl. Acad. Sci. USA 86: 197-201. P. (1986) Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase. DNA 5: 493-501. , Hennig, M. N. (1994) Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase.

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Biochemistry of Vitamin B6 and PQQ by Esmond E. Snell (auth.), G. Marino, G. Sannia, F. Bossa (eds.)

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