Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.64 (MPP)
 1,876 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A putative zinc protease gene operon from Ehrlichia canis was cloned and sequenced. A genomic library was constructed in a pHG165 plasmid vector using Sau3A partially digested E. canis chromosomal DNA. Sequence analysis of the insert DNA from this clone indicated two open reading frames with a size of 1314 and 1350 bp that encodes for ProA and ProB, respectively. Based on BLAST analyses, ProA and ProB share 20-30% identities with members of the eukaryotic mitochondrial processing peptidase (MPP) subfamily, which are heterodimers containing alpha and beta subunits. The subunits share a 20% of identity, but only MPP-beta contains a conserved zincbinding motif, His-Xaa-Xaa-Glu-His (HXXEH). proA and proB are also detectable in E. canis and Ehrlichia chaffeensis, but not the Anaplasma phagocytophila. 5'-RACE revealed that the 5' end of the proA mRNA is heterogeneous, containing additional adenine residues that may be directed by pseudo-templated transcription. Although ProA was identified in both E. canis and E. chaffeensis, ProB was detected only in E. canis. ProA and ProB were both detectable in E. canis-infected DH82 cells. Sera from dogs, which were either naturally or experimentally infected with E. canis, recognized both the recombinant protein antigens.
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PMID:Cloning and characterization of putative zinc protease genes of Ehrlichia canis. 1282 52

We have determined the cDNA sequence encoding bovine mitochondrial ATP-dependent Lon protease. Since the 5'-end region of the cDNA was highly GC-rich and thus could not be amplified by the 5'-RACE method, a genomic DNA fragment containing an in-frame ATG was isolated and sequenced. The translated amino acid sequence contained 961 amino acids with a calculated molecular weight 106,665. Sequence similarities of the bovine enzyme to human and E. coli orthologs were 92 and 27%, respectively. The N-terminal amino acid sequence seemed to be a mitochondrial targeting signal. To determine the cleavage site of the signal sequence we analyzed the mature enzyme purified from bovine adrenocortical mitochondria. Analysis of CNBr-digested peptides revealed that the N-terminus was heterogeneous. We suggest that nonspecific aminopeptidase might remove several amino acids from the N-terminus after mitochondrial processing peptidase has cleaved Gly(67)-Leu(68) or Leu(68)-Trp(69).
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PMID:Nucleotide sequence for cDNA of bovine mitochondrial ATP-dependent protease and determination of N-terminus of the mature enzyme from the adrenal cortex. 1628 28