Characterization of S-adenosylhomocysteine hydrolase from Cryptosporidium parvum.
FEMS Microbiol Lett
; 273(1): 87-95, 2007 Aug.
Article
in En
| MEDLINE
| ID: mdl-17559404
ABSTRACT
The S-adenosylhomocysteine hydrolase from the apicomplexan Cryptosporidium parvum (CpSAHH) has been characterized. CpSAHH is a single-copy, intronless gene of 1479 bp encoding a protein of 493 amino acids with a molecular mass of 55.6 kDa. Reverse transcriptase-polymerase chain reaction analysis confirmed that CpSAHH is expressed both in intracellular stages (in C. parvum-infected HCT-8 cells 24 h after infection) and in sporozoites. CpSAHH was expressed in Escherichia coli TB1 cells as a fusion with maltose-binding protein. The recombinant fusion was cleaved by Factor Xa and the enzymatic activity of both the fusion protein and the purified separated CpSAHH was measured. The enzymatic activity of CpSAHH was inhibited by d-eritadenine, S-DHPA and Ara-A.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Cryptosporidium parvum
/
Adenosylhomocysteinase
Limits:
Animals
Language:
En
Journal:
FEMS Microbiol Lett
Year:
2007
Document type:
Article
Affiliation country:
Czech Republic