Literature DB >> 5961496

Kinetic studies on gluc-amylase. 3. The influence of pH on the rates of hydrolysis of maltose and panose.

K Hiromi, K Takahashi, Z I Hamauzu, S Ono.   

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Year:  1966        PMID： 5961496     DOI： 10.1093/oxfordjournals.jbchem.a128329

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


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  4 in total

1.  pH-dependence of the fast step of maltose hydrolysis catalysed by glucoamylase G1 from Aspergillus niger.

Authors:  U Christensen
Journal:  Biochem J       Date:  2000-07-15       Impact factor: 3.857

2.  Subsite structure and ligand binding mechanism of glucoamylase.

Authors:  K Hiromi; M Ohnishi; A Tanaka
Journal:  Mol Cell Biochem       Date:  1983       Impact factor: 3.396

3.  The glucoamylase of Coniophora cerebella.

Authors:  N J King
Journal:  Biochem J       Date:  1967-11       Impact factor: 3.857

4.  Crystal structure of the starch-binding domain of glucoamylase from Aspergillus niger.

Authors:  Yousuke Suyama; Norifumi Muraki; Masami Kusunoki; Hideo Miyake
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2017-09-23       Impact factor: 1.056
  4 in total

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