PMID:8289297
| Citation |
Alexeev, D, Bury, SM, Boys, CW, Turner, MA, Sawyer, L, Ramsey, AJ, Baxter, HC and Baxter, RL (1994) Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis. J. Mol. Biol. 235:774-6 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1006/jmbi.1994.1030 |
| Keywords |
Amino Acid Sequence; Base Sequence; Biotin/biosynthesis; Carbon-Nitrogen Ligases; Crystallization; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial/genetics; Ligases/chemistry; Ligases/genetics; Molecular Sequence Data |
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