Literature DB >> 37893

Bohr effect in Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions.

N M Allwell, G E Hofmann, A Zaug, M Lennick.   

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Year:  1979        PMID： 37893     DOI： 10.1021/bi00581a016

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


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  4 in total

1.  Mapping structural perturbations in Escherichia coli aspartate transcarbamylase by medium resolution hydrogen exchange.

Authors:  D S Burz; N M Allewell
Journal:  Biophys J       Date:  1986-01       Impact factor: 4.033

2.  The first high pH structure of Escherichia coli aspartate transcarbamoylase.

Authors:  Kimberly A Stieglitz; Jiarong Xia; Evan R Kantrowitz
Journal:  Proteins       Date:  2009-02-01

3.  Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.

Authors:  J W Stebbins; D E Robertson; M F Roberts; R C Stevens; W N Lipscomb; E R Kantrowitz
Journal:  Protein Sci       Date:  1992-11       Impact factor: 6.725

4.  Thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase.

Authors:  M P McCarthy; N M Allewell
Journal:  Proc Natl Acad Sci U S A       Date:  1983-11       Impact factor: 11.205
  4 in total

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