Chondroitin O-methyl ester: an unusual substrate for chondroitin AC lyase.

نویسندگان

  • Fikri Y Avci
  • Toshihiko Toida
  • Robert J Linhardt
چکیده

Chondroitin O-methyl ester was depolymerized by chondroitin AC lyase (EC 4.2.2.5) from Flavobacterium heparinum. The major product isolated from the depolymerization reaction was found to be methyl alpha-L-threo-hex-4-enopyranosyluronate-(1-->4)-2-acetamido-2-deoxy-alpha,beta-D-galactopyranoside.

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Preparation of the methyl ester of hyaluronan and its enzymatic degradation.

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Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis.

The crystal structures of Flavobacterium heparinium chondroitin AC lyase (chondroitinase AC; EC 4.2.2.5) bound to dermatan sulfate hexasaccharide (DS(hexa)), tetrasaccharide (DS(tetra)), and hyaluronic acid tetrasaccharide (HA(tetra)) have been refined at 2.0, 2.0, and 2.1 A resolution, respectively. The structure of the Tyr234Phe mutant of AC lyase bound to a chondroitin sulfate tetrasaccharid...

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عنوان ژورنال:
  • Carbohydrate research

دوره 338 20  شماره 

صفحات  -

تاریخ انتشار 2003