Title : Inverting character of alpha-glucuronidase A from Aspergillus tubingensis - Biely_2000_Biochim.Biophys.Acta_1474_360 |
Author(s) : Biely P , de Vries RP , Vrsanska M , Visser J |
Ref : Biochimica & Biophysica Acta , 1474 :360 , 2000 |
Abstract :
Alpha-glucuronidase A from Aspergillus tubingensis was found to be capable of liberating 4-O-methyl-D-glucuronic acid (MeGlcA) only from those beechwood glucuronoxylan fragments in which the acid is attached to the non-reducing terminal xylopyranosyl residue. Reduced aldotetrauronic acid, 4-O-methyl-D-glucuronosyl-alpha-1,2-D-xylopyranosyl-beta-1,4-xylopyranosyl-beta-1 ,4-xylitol, was found to be a suitable substrate to follow the stereochemical course of the hydrolytic reaction catalyzed by the purified enzyme. The configuration of the liberated MeGlcA was followed in a D(2)O reaction mixture by (1)H-NMR spectroscopy. It was unambiguously established that MeGlcA was released from the substrate as its beta-anomer from which the alpha-anomer was formed on mutarotation. This result represents the first experimental evidence for the inverting character of a microbial alpha-glucuronidase, a member of glycosyl hydrolase family 67 (EC 3.1.1.139). |
PubMedSearch : Biely_2000_Biochim.Biophys.Acta_1474_360 |
PubMedID: 10779688 |
Biely P, de Vries RP, Vrsanska M, Visser J (2000)
Inverting character of alpha-glucuronidase A from Aspergillus tubingensis
Biochimica & Biophysica Acta
1474 :360
Biely P, de Vries RP, Vrsanska M, Visser J (2000)
Biochimica & Biophysica Acta
1474 :360