An extremely thermostable aromatic aminotransferase from the hyperthermophilic archaeon Pyrococcus furiosus-Reference-Cited by-同舟云学术

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An extremely thermostable aromatic aminotransferase from the hyperthermophilic archaeon Pyrococcus furiosus

Published:1995-02 Issue:1 Volume:1247 Page:90-96
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Andreotti Giuseppina,Cubellis Maria Vittoria,Nitti Gianpaolo,Sannia Giovanni,Mai Xuhong,Adams Michael W.W.,Marino Gennaro

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference30 articles.

1. The Purification and Properties of the Aspartate Aminotransferase and Aromatic-Amino-Acid Aminotransferase from Escherichia coli

2. The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes

3. Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli

4. Characterization of amino acid aminotransferases of Methanococcus aeolicus

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