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Gene Review: 

Pmpca  -  peptidase (mitochondrial processing) alpha

Rattus norvegicus

Synonyms: Alpha-MPP, Mitochondrial-processing peptidase subunit alpha, Mppa, P-55
 
 
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Disease relevance of Pmpca

  • Excepting the 1.2-mg diet treatment, maternal weight gains during gestation were greater for P-55 groups compared with gains of the P-115 groups, possibly reflecting maternal growth [1].
  • Both maternal weight gains and fetal weights were less for the 1.2-mg, P-55 group; otherwise reproductive performance was similar among the groups [1].
  • The wild-type and mutated beta-MPPs were co-expressed with alpha-MPP in Escherichia coli [2].
 

High impact information on Pmpca

  • Moreover, the acidified site of alpha-MPP, which binds to the distal basic site in the long presequence, recognized the authentic P(2) arginine as the distal site in compensation for ionic interaction at the proximal site in the mutant MPP [3].
 

Analytical, diagnostic and therapeutic context of Pmpca

  • The purified protease contained two protein subunits of 55 kd (P-55) and 52 kd (P-52) as determined by SDS-PAGE [4].

References

  1. Effects of different levels of pyridoxine fed during pregnancy superimposed upon growth in the rat. Kirksey, A., Pang, R.L., Lin, W.J. J. Nutr. (1975) [Pubmed]
  2. A putative metal-binding site in the beta subunit of rat mitochondrial processing peptidase is essential for its catalytic activity. Kitada, S., Shimokata, K., Niidome, T., Ogishima, T., Ito, A. J. Biochem. (1995) [Pubmed]
  3. Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity. Kitada, S., Yamasaki, E., Kojima, K., Ito, A. J. Biol. Chem. (2003) [Pubmed]
  4. Purification and characterization of a processing protease from rat liver mitochondria. Ou, W.J., Ito, A., Okazaki, H., Omura, T. EMBO J. (1989) [Pubmed]
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