| Literature DB >> 15304318 |
Angel Manteca1, Thilo Kamphausen, Jorg Fanghanel, Gunter Fischer, Jesus Sanchez.
Abstract
Cyclophilins are folding helper enzymes and represent a family of the enzyme class of peptidyl-prolyl cis-trans isomerases. Here, we report the molecular cloning and biochemical characterization of SanCyp18, an 18-kDa cyclophilin from Streptomyces antibioticus ATCC11891 located in the cytoplasm and constitutively expressed during development. Amino acid sequence analysis revealed a much higher homology to cyclophilins from Gram negative bacteria than to known cyclophilins from Streptomyces or other Gram positive bacteria. SanCyp18 is inhibited weakly by CsA, with a K(i) value of 21 microM, similar to cyclophilins from Gram negative bacteria. However, this value is more than 20-fold higher than the K(i) values reported for cyclophilins from other Gram positive bacteria, which makes SanCyp18 unique within this group. The presence of SanCyp18 in Streptomyces is likely due to horizontal gene transmission from Gram-negative bacteria to Streptomyces.Entities:
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Year: 2004 PMID: 15304318 DOI: 10.1016/j.febslet.2004.06.091
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124