RGD Reference Report - A putative metal-binding site in the beta subunit of rat mitochondrial processing peptidase is essential for its catalytic activity. - Rat Genome Database

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A putative metal-binding site in the beta subunit of rat mitochondrial processing peptidase is essential for its catalytic activity.

Authors: Kitada, S  Shimokata, K  Niidome, T  Ogishima, T  Ito, A 
Citation: Kitada S, etal., J Biochem. 1995 Jun;117(6):1148-50.
RGD ID: 13463461
Pubmed: PMID:7490252   (View Abstract at PubMed)

Mitochondrial processing peptidase (MPP) consists of alpha- and beta-subunits (alpha-MPP and beta-MPP). beta-MPP has a putative metal-binding sequence (HXXEH). To determine whether the sequence of beta-MPP is essential for the enzymatic activity, we individually mutated the histidines and glutamic acid to arginines and glutamine, respectively. The wild-type and mutated beta-MPPs were co-expressed with alpha-MPP in Escherichia coli. All three mutants had completely lost the activity, whereas the lost activity was recovered on the addition of wild-type beta-MPP. The activity of the wild-type enzyme was reduced by the mutant beta-MPPs. We conclude from these observations that the HXXEH region is involved in the formation of the active site and that beta-MPP is the catalytic subunit of MPP.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PmpcaRatmetallopeptidase activity contributes_toIDA  RGD 
PmpcbRatmetallopeptidase activity contributes_toIDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Pmpca  (peptidase, mitochondrial processing subunit alpha)
Pmpcb  (peptidase, mitochondrial processing subunit beta)


Additional Information