Literature DB >> 7059572

Stopped-flow kinetic studies on the binding of gluconolactone and maltose to glucoamylase.

A Tanaka, M Ohnishi, K Hiromi.   

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Year:  1982        PMID： 7059572     DOI： 10.1021/bi00530a019

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


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  3 in total

1.  Presteady-state kinetics of Bacillus 1,3-1,4-beta-glucanase: binding and hydrolysis of a 4-methylumbelliferyl trisaccharide substrate.

Authors:  M Abel; A Planas; U Christensen
Journal:  Biochem J       Date:  2001-07-01       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.  Pre-steady-state kinetics of Bacillus licheniformis 1,3-1,4-beta-glucanase: evidence for a regulatory binding site.

Authors:  Mireia Abel; Karin Iversen; Antoni Planas; Ulla Christensen
Journal:  Biochem J       Date:  2003-05-01       Impact factor: 3.857
  3 in total

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