Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis.
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.
Alexeev
D
D
Department of Biochemistry, University of Edinburgh, Scotland.
Bury
S M
SM
Boys
C W
CW
Turner
M A
MA
Sawyer
L
L
Ramsey
A J
AJ
Baxter
H C
HC
Baxter
R L
RL
D000595:Amino Acid Sequence; D001483:Base Sequence; D001710:Biotin / Q000096:biosynthesis; D019731:Carbon-Nitrogen Ligases; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics; D008025:Ligases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data
D001710:Biotin; D008025:Ligases; D019731:Carbon-Nitrogen Ligases; C020024:dethiobiotin synthetase