Literature DB >> 8289297

Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis.

D Alexeev1, S M Bury, C W Boys, M A Turner, L Sawyer, A J Ramsey, H C Baxter, R L Baxter.   

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.

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Year:  1994        PMID: 8289297     DOI: 10.1006/jmbi.1994.1030

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon.

Authors:  S Bower; J B Perkins; R R Yocum; C L Howitt; P Rahaim; J Pero
Journal:  J Bacteriol       Date:  1996-07       Impact factor: 3.490

2.  An embryo-defective mutant of arabidopsis disrupted in the final step of biotin synthesis

Authors: 
Journal:  Plant Physiol       Date:  1998-03       Impact factor: 8.340

  2 in total

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