53313-95-4Relevant articles and documents
Mutasynthesis of Glycopeptide Antibiotics: Variations of Vancomycin's AB-Ring Amino Acid 3,5-Dihydroxyphenylglycine
Weist, Stefan,Kittel, Claudia,Bischoff, Daniel,Bister, Bojan,Pfeifer, Volker,Nicholson, Graeme J.,Wohlleben, Wolfgang,Suessmuth, Roderich D.
, p. 5942 - 5943 (2007/10/03)
In the mutasynthetic approach, the ΔdpgA mutant of the vancomycin-type glycopeptide antibiotic producer Amycolatopsis balhimycina, which is deficient in the synthesis of 3,5-dihydroxyphenylglycine (DPg), was supplemented with synthetic DPg analogues to obtain the corresponding modified glycopeptides. Sterically more demanding 3,5-disubstituted methoxy derivatives as well as monosubstituted DPg analogues were accepted as substrates. These facts indicate that steric and electronic requirements suffice in several cases for the oxidative closure of the AB ring, thus leading to the generation of novel antibiotically active glycopeptide derivatives. The results represent a further step in evaluating the potential of mutasynthesis for peptidic secondary metabolites. Copyright
Synthesis and antimicrobial activity of some heterocyclic compounds
Trivedi, P. B.,Undavia, N. K.,Dave, A. M.,Bhatt, K. N.,Desai, N. C.
, p. 497 - 500 (2007/10/02)
Condensation of 2-phenyl-3-(4-benzoyl hydride)-1,3-quinazolin-4(4H)-one (1) with various aldehydes gives 2-phenyl-3-(4-arylidene-benzoylhydrazide)-1,3-quinazolin-4(4H)-one (II), which on cycloaddition with mercaptoacetic acid yield 4-thiazolidinones (IIIa-o).Compound (I) on treatment with aromatic cyanohydrines and aryl isothiocyanates gives α-carbohydrazino nitriles of (IVa-m) and thiosemicarbazides (Va-l) respectively.The structures of III-V have been elucidated on the basis of their elemental analysis and spectral data.These compounds exhibit moderate to goodantibacterial and tuberculostatic activities.
Hydroxynitrile lyases from almond and sorghum as biocatalysts
Smitskamp-Wilms, E.,Brusse, J.,Gen, A. van der,Scharrenburg, G.J.M. van,Sloothaak, J. B.
, p. 209 - 215 (2007/10/02)
Hydroxynitrile lyases from sweet almond (E.C.4.1.2.10) and from sorghum biocolor (E.C.4.1.2.11) have been purified to homogeneity by ion-exchange chromatography.These enzymes catalyse the decomposition of α-hydroxynitriles to aldehydes and hydrocyanic acid (HCN) and show great promise for synthetic applications in the reverse reaction: the stereospecific addition of HCN to aldehydes to form enantio-pure α-hydroxynitriles.Physical and kinetic characteristics of the two dominating isoenzymes in each source were compared and revaled appreciable species-specific differences in substrate specificity between iso forms within one species, were, however, found to be small.The native molecular weight for the sorghum lyase was found to be 95kDa.This is in contrast with an earlier reported value of 180 kDa.From the kinetic parameters Km and Vmax, a specificity constant was calculated, which can be used to predict the potential application of oxynitrilase as a biocatalyst for specific synthetic purposes.
