Literature DB >> 4213409

Subsite affinities of bacterial liquefying alpha-amylase evaluated from the rate parameters of linear substrates.

S Iwasa, H Aoshima, K Hiromi, H Hatano.   

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Year:  1974        PMID： 4213409     DOI： 10.1093/oxfordjournals.jbchem.a130499

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


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  4 in total

1.  Subsite mapping of enzymes. Depolymerase computer modelling.

Authors:  J D Allen; J A Thoma
Journal:  Biochem J       Date:  1976-10-01       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.  Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences.

Authors:  K Igarashi; Y Hatada; H Hagihara; K Saeki; M Takaiwa; T Uemura; K Ara; K Ozaki; S Kawai; T Kobayashi; S Ito
Journal:  Appl Environ Microbiol       Date:  1998-09       Impact factor: 4.792

4.  Active site studies on Bacillus amyloliquefaciens alpha-amylase (I).

Authors:  R D Dua; S Kochhar
Journal:  Mol Cell Biochem       Date:  1985-02       Impact factor: 3.396
  4 in total

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