Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis
| Autor: | M.A. Turner, A.J. Ramsey, H. C. Baxter, Dmitriy Alexeev, R.L. Baxter, C.W.G. Boys, Lindsay Sawyer, Stella M. Bury |
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| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
Biotin medicine.disease_cause Dethiobiotin synthase Ligases chemistry.chemical_compound Structural Biology medicine Escherichia coli Carbon-Nitrogen Ligases Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification biology Base Sequence Nucleic acid sequence biology.organism_classification Enterobacteriaceae Enzyme chemistry Biochemistry Genes Bacterial biology.protein Crystallization Bacteria |
| Zdroj: | Journal of molecular biology. 235(2) |
| ISSN: | 0022-2836 |
| Popis: | The enzyme dethiobiotin synthetase (EC 6.3.3.3) has been cloned and over-expressed in Escherichia coli in such a way that milligram quantities are available. The purified enzyme has been subjected to a number of physical and chemical studies, sequenced and most notably it has been crystallized in a form that is suitable for X-ray structure determination. The cell dimensions are a = 72.8 A, b = 49.2 A, c = 61.4 A, beta = 106.2 degrees. The systematic absences are consistent with the monoclinic space group C2 with one polypeptide chain in the asymmetric unit. |
| Databáze: | OpenAIRE |
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