期刊
FEBS LETTERS
卷 467, 期 2-3, 页码 333-336出版社
WILEY
DOI: 10.1016/S0014-5793(00)01173-X
关键词
endopolygalacturonase; processivity; methylated oligogalacturonate; Aspergillus niger
We isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, from Aspergillus niger. The primary structure of PGD differs from that of other A, niger PGs by a 136 amino acid residues long N-terminal extension. Biochemical analysis demonstrated extreme processive behavior of the enzyme on oligomers longer than five galacturonate units. Furthermore, PGD is the only A. niger PG capable of hydrolyzing di-galacturonate. It is tentatively concluded that the enzyme is composed of four subsites, The physiological role of PGD is discussed. (C) 2000 Federation of European Biochemical Societies.
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