3.4.24.64: mitochondrial processing peptidase
This is an abbreviated version!
For detailed information about mitochondrial processing peptidase, go to the full flat file.
Reaction
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
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Synonyms
Alpha-MPP, Atp23, Beta-MPP, EC 3.4.99.41, General mitochondrial processing peptidase, GPP, HA1523, HPP, Imp1, Imp2, inner membrane peptidase processing enzyme, Mas1, Mas2, Matrix peptidase, Matrix processing peptidase, Matrix processing proteinase, Mitochondrial chelator-sensitive protease, mitochondrial processing peptidase, mitochondrial processing peptidase-alpha protein, mitochondrial processing protease, Mitochondrial protein precursor-processing proteinase, MMP-beta, More, MPP, MPP-alpha, P-52, P-55, PEP, Plsp1, Plsp2, PMPCA, Processing enhancing peptidase, processing enhancing protein, processing peptidase, Proteinase, mitochondrial protein precursor-processing, thylakoidal processing peptidase, TPP, TTHA1264
ECTree
Metals Ions
Metals Ions on EC 3.4.24.64 - mitochondrial processing peptidase
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Mg2+
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divalent cation required for enzyme activity
Co2+
-
divalent cation required for enzyme activity
Co2+
-
requirement (in vitro, in vivo not identified yet)
Co2+
-
activation of chelator-inactivated enzyme
Fe2+
-
divalent cation required for enzyme activity
Fe2+
-
the N-terminus of MPP-processed frataxin shows a unique high-affinity iron site, and this iron center appears to mediate a self-cleavage reaction, the N-terminus blocks previously defined iron-binding sites located on the carboxylate-rich surface defined by the helix alpha1 and the beta-sheet beta1, most likely through electrostatic contact with the carboxylate-rich surface on the core protein, as well as inhibiting iron-promoted binding of the iron-sulfur cluster assembly scaffold partner protein, ISU, overview
Mn2+
-
divalent cation required for enzyme activity
Mn2+
-
requirement (in vitro, in vivo not identified yet)
Zn2+
-
the proteolytic subunit contains a zinc-binding catalytic site
Zn2+
-
divalent cation required for enzyme activity
Zn2+
-
zinc binding motif in beta-MPP
Zn2+
-
activation of chelator-inactivated enzyme
Zn2+
-
localized in the active site cavity
Zn2+
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zinc binding motif in beta-MPP
Zn2+
-
MPP is a zinc-metalloendopeptidase
Zn2+
a zinc-metallopeptidase, the betaMPP subunit contains the zinc-binding motif, HxxEHx74E, essential for peptidase activity
Zn2+
-
the enzyme binds zinc
Zn2+
-
zinc-dependent metallopeptidase
additional information
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GPP is a metallopeptidase
additional information
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metalloendopeptidase that does not contain His-Glu-X-X-His zinc-binding motif, cf. human insulinase or E. coli protease III
additional information
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no activation by Ca2+, Mg2+, Cu2+, Ni2+ or Fe2+
additional information
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metalloendopeptidase that does not contain His-Glu-X-X-His zinc-binding motif, cf. human insulinase or E. coli protease III
additional information
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atomic absorption spectroscopy: purified MAS1/MAS2-holoenzyme lacks significant amounts of zinc, manganese or cobalt, probably lost during purification
additional information
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consensus metal-binding motif HEliH, formed by amino acid residues 167-171 of Atp23
additional information
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no externally added metal ions required
additional information
-
no externally added metal ions required