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.
Word Map on EC 3.4.24.64
-
3.4.24.64
-
presequence
-
nuclear-encoded
-
preproteins
-
intermembrane
-
frataxin
-
metalloendopeptidase
-
friedreich
-
matrix-targeting
-
hxxeh
-
mas1
-
plumbaginifolia
-
nuclearly
-
matrix-localized
-
intermediate-sized
-
agriculture
- 3.4.24.64
- presequence
-
nuclear-encoded
- preproteins
-
intermembrane
- frataxin
- metalloendopeptidase
-
friedreich
-
matrix-targeting
-
hxxeh
- mas1
- plumbaginifolia
-
nuclearly
-
matrix-localized
-
intermediate-sized
- agriculture
Reaction
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 =
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
3.4.24.64 mitochondrial processing peptidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.24.64 - mitochondrial processing peptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
delW481-F482
-
mutation has no effect on protein solubility, slightly unstable during long-term storage
E168Q
-
site-directed mutation in the consensus metal-binding site, the active site residue mutant is proteolytically inactive, but shows processing of the Atp6 subunit of pre-F1FO-ATP synthase
E73Q
H167A
-
site-directed mutation in the consensus metal-binding site, the mutant does not show processing of the Atp6 subunit of pre-F1FO-ATP synthase
H171A
-
site-directed mutation in the consensus metal-binding site, the mutant does not show processing of the Atp6 subunit of pre-F1FO-ATP synthase
additional information
E73Q
-
site-directed mutagenesis, active site mutant, forms dimers like the wild-type enzyme
additional information
construction of alphaMPP237-GFP, a fusion protein in which the N-terminal 237 amino acids of alpha-MPP are fused to GFP for subcellular localization study
additional information
-
construction of alphaMPP237-GFP, a fusion protein in which the N-terminal 237 amino acids of alpha-MPP are fused to GFP for subcellular localization study
additional information
-
yeast malate dehydrogenase and human, yeast, or rat liver aldehyde dehydrogenases are mutated so that they would not be processed by the enzyme after import into the mitochondrial matrix space, the mutant nonprocessed enzymes are functional but instable, the nonprocessed precursors are degraded in the matrix space, expression in HeLa cells, overview
additional information
-
construction of a EGFP fused to a yeast aconitase presequence and 7-dietylamino-3-(4'-maleimidyl phenyl)-4-methyl coumarin-labelled yeast MPPs for fluorescence resonance energy transfer analysis
additional information
-
deletion of ATP23 completely inhibits the assembly of the mitochondrial-encoded FO-subunits into the F1FO-ATP synthase, which is observed in wild-type mitochondria
additional information
-
yeast aldehyde dehydrogenase and malate dehydrogenase are mutated so that they would not be processed by the enzyme after import into the mitochondrial matrix space, the mutant nonprocessed enzymes are functional but instable, the nonprocessed precursors are degraded in the matrix space, expression in HWTHL10 cells, overview
