Information on EC 3.4.24.B19 - i-AAA protease

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.4.24.B19
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
i-AAA protease
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
405910-55-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain W303-1A
-
-
Manually annotated by BRENDA team
additional information
expressed from pRS314 vector
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
constitutive OPA1 cleavage by YME1L and OMA1 at two distinct sites leads to the accumulation of both long and short forms of OPA1 and maintains mitochondrial fusion
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Aim37 + H2O
?
show the reaction diagram
-
-
-
-
?
Cox2 + H2O
?
show the reaction diagram
-
-
-
-
?
DnaX + H2O
?
show the reaction diagram
-
the enzyme partially degrades DnaX to produce stable fragments upon encountering a glycine-rich region adjacent to a structured domain
-
-
?
Erv1 + H2O
?
show the reaction diagram
-
-
-
-
?
Fcj1 + H2O
?
show the reaction diagram
-
-
-
-
?
hybrid protein of subunit 2 of cytochrome oxidase residues 1-74, mouse dihydrofolate reductase, and mitochondrial presequence, residues 1-66, of subunit 9 of the ATPase of Neurospora crassa + H2O
4 peptide fragments f1-f4
show the reaction diagram
-
in vitro import into the mitochondrion
product characterization
?
KAENQKARFSDVHGC + H2O
?
show the reaction diagram
-
-
-
-
?
loosely folded Yta10(161)-dihydrofolate reductase + H2O
?
show the reaction diagram
-
in vitro import into mitochondria, not intact wild-type dihydrofolate reductase
-
?
Mcs10 + H2O
?
show the reaction diagram
-
-
-
-
?
Mcs27 + H2O
?
show the reaction diagram
-
-
-
-
?
Mio10 + H2O
?
show the reaction diagram
-
-
-
-
?
Mos1 + H2O
?
show the reaction diagram
-
-
-
-
?
Mpm1 + H2O
?
show the reaction diagram
-
-
-
-
?
Nde1 + H2O
?
show the reaction diagram
-
-
-
-
?
Nde1p + H2O
?
show the reaction diagram
-
-
-
-
?
OPA1 + H2O
?
show the reaction diagram
polynucleotide phosphorylase + H2O
?
show the reaction diagram
-
Yme1 is required for PNPase assembly in the intermembrane space
-
-
?
prohibitin + H2O
?
show the reaction diagram
-
-
-
-
?
protein + H2O
peptides
show the reaction diagram
protein Cox2 + H2O
?
show the reaction diagram
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
proteins + H2O
peptides
show the reaction diagram
-
-
?
receptor protein Atg32 + H2O
?
show the reaction diagram
-
-
-
-
?
residues 1-74 of subunit 2 of cytochrome oxidase + H2O
?
show the reaction diagram
-
two-step procedure, in vitro import into the mitochondrion
-
?
subunit 2 of cytochrome c oxidase + H2O
?
show the reaction diagram
-
-
-
-
?
unassembled cytochrome oxidase 2
?
show the reaction diagram
-
-
-
?
unassembled gamma subunit of mitochondrial ATP-synthase + H2O
?
show the reaction diagram
-
i.e. Atp3p
-
?
unassembled subunit II of cytochrome oxidase + H2O
?
show the reaction diagram
-
i.e. Cox2p
-
?
Ups2 + H2O
?
show the reaction diagram
-
-
-
-
?
Yta10(161)-DHFRmut + H2O
?
show the reaction diagram
-
-
-
-
?
Cox2 + H2O
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Aim37 + H2O
?
show the reaction diagram
-
-
-
-
?
Cox2 + H2O
?
show the reaction diagram
-
-
-
-
?
DnaX + H2O
?
show the reaction diagram
-
the enzyme partially degrades DnaX to produce stable fragments upon encountering a glycine-rich region adjacent to a structured domain
-
-
?
Erv1 + H2O
?
show the reaction diagram
-
-
-
-
?
Fcj1 + H2O
?
show the reaction diagram
-
-
-
-
?
Mcs10 + H2O
?
show the reaction diagram
-
-
-
-
?
Mcs27 + H2O
?
show the reaction diagram
-
-
-
-
?
Mio10 + H2O
?
show the reaction diagram
-
-
-
-
?
Mos1 + H2O
?
show the reaction diagram
-
-
-
-
?
Mpm1 + H2O
?
show the reaction diagram
-
-
-
-
?
Nde1 + H2O
?
show the reaction diagram
-
-
-
-
?
OPA1 + H2O
?
show the reaction diagram
-
YME1L cleaves OPA1 at S2
-
-
?
prohibitin + H2O
?
show the reaction diagram
-
-
-
-
?
protein + H2O
peptides
show the reaction diagram
protein Cox2 + H2O
?
show the reaction diagram
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
proteins + H2O
peptides
show the reaction diagram
P32795
-
-
?
receptor protein Atg32 + H2O
?
show the reaction diagram
-
-
-
-
?
unassembled cytochrome oxidase 2
?
show the reaction diagram
-
-
-
?
unassembled gamma subunit of mitochondrial ATP-synthase + H2O
?
show the reaction diagram
-
i.e. Atp3p
-
?
unassembled subunit II of cytochrome oxidase + H2O
?
show the reaction diagram
-
i.e. Cox2p
-
?
Ups2 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activity with beta-gamma-imidoadenosine 5'-phosphate, i.e. AMP-PNP
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
-
-
methotrexate
-
inhibits binding of the protein substrate to the enzyme's AAA domain
o-phenanthroline
-
strong
proteinase K
-
-
-
additional information
-
no inhibition by prohibitin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mgr1p
-
Mgr3p and Mgr1p can bind substrate even in the absence of Yme1p, and both proteins are needed for maximal binding of an unfolded substrate by the i-AAA complex. Mgr3p and Mgr1p function together in an adaptor complex that seems to help target substrates to the i-AAA protease for degradation
-
Mgr3p
-
Mgr3p and Mgr1p can bind substrate even in the absence of Yme1p, and both proteins are needed for maximal binding of an unfolded substrate by the i-AAA complex. Mgr3p and Mgr1p function together in an adaptor complex that seems to help target substrates to the i-AAA protease for degradation
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
-
x * 71000, mature protein, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
YME1L is a stress-sensitive mitochondrial protease that is rapidly degraded in response to acute oxidative (0.2 mM H2O2) stress
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
-
purification of recombinant GST-fusion AAA-domain N-terminal fragment from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Mus musculus
-
expressed in SHSY5Y cells
-
expression of N-terminal residues 250-313 of the AAA domain as GST-fusion protein in Escherichia coli
-
expression of wild-type and mutant E41Q in deficient mutant cell DELTAyme1, complementation only by the wild-type
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expression of wild-type enzyme in Escherichia coli strain DH5alpha, expression of deletion mutant in Escherichia coli strain BMH 71-18 mut S
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expressed in deltayme1 yeast strain
additional information
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E540Q
-
inactive
K327R
-
point mutation at the ATP-binding site, catalytically inactive
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation