scholarly journals Preliminary Characterization of an Antibiotic Produced by Xanthomonas albilineans Which Inhibits DNA Synthesis in Escherichia coli

Microbiology ◽  
1985 ◽  
Vol 131 (5) ◽  
pp. 1069-1075 ◽  
Author(s):  
R. G. BIRCH ◽  
S. S. PATIL
Keyword(s):  
Escherichia Coli ◽  
Dna Synthesis ◽  
Preliminary Characterization ◽  
Xanthomonas Albilineans

scholarly journals The 8-amino-7-oxopelargonate synthase from Bacillus sphaericus. Purification and preliminary characterization of the cloned enzyme overproduced in Escherichia coli

1992 ◽  
Vol 283 (2) ◽  
pp. 327-331 ◽  
Author(s):  
O Ploux ◽  
A Marquet
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Absorption Band ◽  
Specific Activity ◽  
Bacillus Sphaericus ◽  
Complete Agreement ◽  
Amino Acid Residues ◽  
Characteristic Absorption Band ◽  
Preliminary Characterization

The 8-amino-7-oxopelargonate synthase [6-carboxyhexanoyl-CoA:L-alanine carboxyhexanoyltransferase (decarboxylating); EC 2.3.1.47] from Bacillus sphaericus involved in biotin biosynthesis was purified from an Escherichia coli overproducing strain. The purification afforded an electrophoretically homogeneous enzyme with a specific activity of 0.67 unit/mg. The purified enzyme is a monomer of 41 kDa. N-Terminal sequencing of the first 14 amino acid residues showed complete agreement with the predicted sequence from the bioF gene. The pure enzyme showed the characteristic absorption band (425 nm) of pyridoxal 5′-phosphate-dependent enzymes. Furthermore, the holoenzyme was resolved during an affinity step yielding the inactive apoenzyme, which recovered activity and the 425 nm-absorption band on dialysis against pyridoxal 5′-phosphate. Km values for L-alanine and pimeloyl-CoA were respectively 3 mM and 1 microM.

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