Literature DB >> 2364940

Conformational studies on the N-linked carbohydrate chain of bromelain.

J B Bouwstra1, E C Spoelstra, P De Waard, B R Leeflang, J P Kamerling, J F Vliegenthart.   

Abstract

1H- and 13C-NMR assignments for the carbohydrate part of the glycopeptide alpha-D-Man-(1----6)-[beta-D-Xyl-(1----2)]-beta-D-Man-(1----4)-beta-D- GlcNAc-(1----4)-[alpha-L-Fuc-(1----3)]-beta-D-GlcNAc-(1----N)-Asn approximately, derived from the proteolytic enzyme bromelain (EC 3.4.22.4), have been obtained using homo- and heteronuclear correlation spectroscopy, two-dimensional homonuclear Hartmann-Hahn and nuclear Overhauser enhancement experiments. A conformational model for the carbohydrate chain, deduced from the NMR data and consistent with hard-sphere exo-anomeric calculations shows that the rotamer population about the C-5--C-6 bond of beta-Man is restricted to the P omega = 180 rotamer, mainly.

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Year:  1990        PMID： 2364940     DOI： 10.1111/j.1432-1033.1990.tb15553.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  16 in total

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7.  Circular dichroism of stem bromelain: a third spectral class within the family of cysteine proteinases.

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