Cyanide hydrolysis is a cyanide-degrading bacterium, Pseudomonas stutzeri AK61, by cyanidase

Article Abstract:

A study was conducted to characterize the isolation of a cyanide-degrading bacterium from the waste water of a metal-plating facility, and to describe the cyanide-degrading enzyme resulting from the strain. Cultivation in an isolation medium with 1 mM KCN was utilized to carry out the isolation procedure. Results indicated that the enzyme was characterized by one kind of polypeptide. Findings also showed that enzyme activity was significantly influenced by the addition of Hg2+ at a concentration of 0.1 mM.

author: Watanabe, Atsushi, Karube, Isao, Yano, Kazuyoshi, Ikebukuro, Kazunori
Cyanides

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pBLA8, from Brevibacterium linens, belongs to a Gram-positive subfamily of CoIE2-related plasmids

Article Abstract:

A 3.1 kb DNA segment from the Brevibacterium linens cryptic plasmid pBLA8 has been cloned and sequenced. It contains information needed for autonomous replication. It is distinguished by the presence of an ori site upstream of an operon encoding the RepA and RepB proteins, required for replication. pBLA8 was assigned to a new CoIE21 subfamily which requires two Rep proteins and the location of an ori site upstream of the repAB operon.

author: Blanco, Carlos, Rince, Alain, Leret, Veronique, Trautwetter, Annie
Plasmids

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The fructokinase from Rhizobium leguminosarum biovar trifolii belongs to group I fructokinase enzymes and is encoded separately from other carbohydrate metabolism enzymes

Article Abstract:

The nucleotide sequence of the fructokinase gene from Rhizobium leguminosarum biovar trifolii BAL, the deduced amino acid sequence and similarities to other known fructokinases are reported. The fructokinase enzyme was purified to electrophoretic homogeneity and was characterized in part. The fructokinase protein's N-terminal amino acid sequence was determined, leading to a confirmation of the gene sequence reported.

author: Fennington, George J., Jr., Hughes, Thomas A.
Carbohydrate metabolism

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subjects list: Research, Enzymes, Bacteria
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