Open AccessConformational studies on the N‐linked carbohydrate chain of bromelain
Author(s) -
BOUWSTRA Jan B.,
SPOELSTRA Ellen C.,
WAARD Pieter,
LEEFLANG Bastiaan R.,
KAMERLING Johannis P.,
VLIEGENTHART Johannes F. G.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb15553.x
Subject(s) - heteronuclear molecule , homonuclear molecule , conformational isomerism , chemistry , anomer , nuclear overhauser effect , stereochemistry , glycopeptide , carbohydrate , nuclear magnetic resonance spectroscopy , bromelain , chain (unit) , population , crystallography , enzyme , molecule , biochemistry , physics , organic chemistry , medicine , antibiotics , environmental health , astronomy , protease
1 H‐ and 13 C‐NMR assignments for the carbohydrate part of the glycopeptide α‐ d ‐Man‐(1→6)‐[ß‐ d ‐Xyl‐(1→2)]‐ß‐ d ‐Man‐(1→4)‐ß‐ d ‐GlcNAc‐(1→4)‐[α‐ l ‐Fuc‐(1→3)]‐ß‐ d ‐ GlcNAc‐(1→N)‐Asn∼, 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 ß‐Man is restricted to the P ω = 180 rotamer, mainly.