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Literature summary for 3.4.24.64 extracted from

  • Emmermann, M.; Braun, H.P.; Arretz, M.; Schmitz, U.K.
    Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria (1993), J. Biol. Chem., 268, 18936-18942.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Solanum tuberosum
Solanum tuberosum, subunits I-III Solanum tuberosum

General Stability

General Stability Organism
Highly salt resistant, optimum at 0.9 M, still active at 1.5 M NaCl Solanum tuberosum
Separation of subunit III from cytochrome reductase-processing peptidase complex leads to aggregation of the remaining subcomplex and irreversible loss of processing activity Solanum tuberosum

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Solanum tuberosum 16020
-
mitochondrion
-
Solanum tuberosum 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no externally added metal ions required Solanum tuberosum

Organism

Organism UniProt Comment Textmining
More
-
the enzymes from Spinacia oleracea or Solanum tuberosum are immunologically not related to MPP but to processing enhancing protein (i.e. PEP) from fungi and mammals
-
Solanum tuberosum
-
var. Marfona
-

Reaction

Reaction Comment Organism Reaction ID
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 mechanism Solanum tuberosum
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 structure-function relationship Solanum tuberosum

Source Tissue

Source Tissue Comment Organism Textmining
tuber
-
Solanum tuberosum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
F1-ATPase beta-subunit precursor + H2O F0F1-ATP-synthase F1beta subunit precursor from Nicotiana plumbaginifolia Solanum tuberosum F1-ATPase beta-subunit
-
?
F1-ATPase beta-subunit precursor + H2O no cleavage with isolated enzyme subunits Solanum tuberosum F1-ATPase beta-subunit
-
?
additional information plant enzyme is integral part of bifunctional cytochrome c reductase complex Solanum tuberosum ?
-
?
additional information neither the individual subunits nor their combinations are catalytically active in in vitro processing Solanum tuberosum ?
-
?
P53 precursor + H2O i.e. subunit II of cytochrome c reductase complex, cleavage site: Tyr32-Ser33 Solanum tuberosum P53
-
?
P55 precursor + H2O i.e. subunit I of cytochrome c reductase complex, cleavage site: Ser32-Ser33 Solanum tuberosum P55
-
?

Subunits

Subunits Comment Organism
More sequence homologies between P55, P53 from potato and processing enhancing protein from yeast or Neurospora crassa and between P51 from potato and MPP from yeast or Neurospora crassa Solanum tuberosum
More the mitochondrial processing peptidase components of cytochrome c reductase-processing peptidase complex are the three largest subunits: P55, P53 and P51, with MW 55000, 53000 and 51000, respectively, SDS-PAGE Solanum tuberosum