Literature DB >> 307963

Multimolecular substrate reactions catalyzed by caabohydrases. Aspergillus oryzae alpha-amylase degradation of maltooligosaccharides.

J D Allen, J A Thoma.   

Abstract

Aspergillus oryzae alpha-amylase degrades maltooligosaccharides by other pathways besides simple glycosidic bond scission. The utilization of the alternate pathways increases with the concentration of substrate implicating a multimolecular substrate mechanism. Reducing-end labeled and uniformly labeled maltooligosaccharides were used to elucidate these alternate degradation mechanisms. Condensation followed by hydrolysis is not a significant pathway. Transglycosylation is concluded to occur, but no single transglycosylation mechanism can account for all of the experimental data for maltotriose degradation. Rather, a combination of transglycosylations must be invoked.

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Year:  1978        PMID: 307963     DOI: 10.1021/bi00605a013

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  3 in total

1.  Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose.

Authors:  Jie Zhou; Zhoukun Li; Han Zhang; Jiale Wu; Xianfeng Ye; Weiliang Dong; Min Jiang; Yan Huang; Zhongli Cui
Journal:  Appl Environ Microbiol       Date:  2018-07-02       Impact factor: 4.792

2.  The xylan-degrading enzyme system of Talaromyces emersonii: novel enzymes with activity against aryl beta-D-xylosides and unsubstituted xylans.

Authors:  M G Tuohy; J Puls; M Claeyssens; M Vrsanská; M P Coughlan
Journal:  Biochem J       Date:  1993-03-01       Impact factor: 3.857

3.  Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes S85.

Authors:  H Zhu; F W Paradis; P J Krell; J P Phillips; C W Forsberg
Journal:  J Bacteriol       Date:  1994-07       Impact factor: 3.490

  3 in total

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