• Journal of Life Science
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• v.8 no.6
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• pp.673-680
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• 1998

Adenosine deaminase gene from Nocardioides sp. J-326TK was cloned by polymerase chain reaction using primers (PI, PII and PIII) constructed from the highly conserved amino acid sequences among Escherichia coli, mouse and human. A PCR product of about 800bp, as expected from the sequence of E. coli adenosine deaminase gene, was obtained from Nocardioides sp. J-326TK chromosomal DNA double-digested with EcoRI and Pst I. DNA sequencing of the PCR product after cloning into pT7Blue T-vector shows 99.5% and 98.9% homologies in nucleotide and amino acid sequences, respectively, with the E. coli adenosine deaminase whereas 59.5% and 46.8% homologies with the human adenosine deaminase, indicating the evolutionarily relationship of these organisms.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.83-89
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• 1990

Two strains of actinomycetes producing extracellular adenosine deaminase, strain J-845S and strain J-326TK, were isolated from soil. Strain J-845S was gram-positive and non-acid-fast. This strain formed whitish, rod-shaped, smooth and non-motile spores on the aerial mycelium, and the spore chain was spiral. The hyphae of the mycelium branched abundantly. Cell wall chemotypes of the strain were of type I containing LL-diaminopimelic acids, and of phospholipid type II, and then strain J-845S was designated as Streptomyces sp.. Strain J-326TK was gram-positive and non-acid-fast. The hyphae of primary and aerial mycelium fragmented into irregular rod of coccus-like elements. The aerial mycelium either did not branch or sparsely branched. Cell wall composition was of type I and phospholipid type I. Thus, strain J-326TK was identified as Nocardioides sp.

• Journal of Life Science
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• v.9 no.1
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• pp.64-68
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• 1999

The properties of purified intracellular adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) of Nocardioides sp. J-326TK isolated from soil have been studied. The enzyme deaminated adenosine and 2`-deoxyadenosine and the respective {TEX}$K_{M}${/TEX} values were 4.0×{TEX}$10^{-4}${/TEX} M and 5.0× {TEX}$10^{-4}${/TEX} M, but the enzyme was not active on 8-bromoadenosine, 6-methylaminopurine riboside, ATP, ADP, 2`-AMP, 3`-AMP, 5`-AMP, dAMP, cAMP, NAD, FAD, NADP and adenine. The enzyme activity was strongly inhibited by the addition of {TEX}$Hg^{2+}${/TEX} and {TEX}$Ag^{+}${/TEX}, {TEX}$Cu^{2+}${/TEX}, {TEX}$Co^{2+}${/TEX} and {TEX}$Mn^{2+}${/TEX} also inhibited the activity but much less extent. The effect of alkyl reagents, metal chelating reagents and certain other compounds on the enzyme activity were also examined. No reagent activated the enzyme. On the contrary, the enzyme reaction was slightly inhibited by o-phenanthroline and 6-benzyladenosine.