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Information on EC 3.4.21.53 - Endopeptidase La and Organism(s) Homo sapiens and UniProt Accession P36776

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.53 Endopeptidase La
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This record set is specific for:
Homo sapiens
UNIPROT: P36776 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hydrolysis of proteins in presence of ATP
Synonyms
protease, serine protease, clpxp, lon protease, lonp1, protease la, atp-dependent lon protease, protease lon, aaa+ protease, ms-lon, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
human ATP-dependent protease
-
human lon protease
-
LON protease 1
-
mitochondrial ATP-dependent protease La
-
mitochondrial Lon protease
-
Protease La
-
ATP-dependent lon protease
-
-
ATP-dependent Lon proteinase
-
-
-
-
ATP-dependent protease La
-
-
-
-
ATP-dependent serine proteinase
-
-
-
-
Escherichia coli proteinase La
-
-
-
-
Escherichia coli serine proteinase La
-
-
-
-
Gene lon protease
-
-
-
-
Gene lon proteins
-
-
-
-
lon ATP-dependent protease
-
-
Lon protein
-
-
Lon proteinase
-
-
-
-
lonA
-
-
LONP1
-
-
PIM1 protease
-
-
-
-
PIM1 proteinase
-
-
-
-
Protease La
Proteinase La
-
-
-
-
Proteinase, Escherichia coli serine, La
-
-
-
-
Proteinase, La
-
-
-
-
Proteins, gene lon
-
-
-
-
Proteins, specific or class, gene lon
-
-
-
-
Serine protease La
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
79818-35-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-aminolevulinic acid synthase + H2O
?
show the reaction diagram
-
-
-
?
Abf2 + H2O
?
show the reaction diagram
a yeast mitochondrial protein, homologuous to human mitochondrial TFAM protein. The substrate is protected from degradation when bound to a nucleic acid. Abf2 associates with both types of DNA, dsDNA and ssDNA
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
cystathionine beta-synthase + H2O
?
show the reaction diagram
when misfolded or unfolded
-
-
?
cytochrome c oxidase 4 isoform 1 + H2O
?
show the reaction diagram
i.e. COX4-1
-
-
?
FRETN 89-98 + H2O
?
show the reaction diagram
-
-
-
?
Glu-Ala-Ala-Phe-4-methoxy-2-naphthylamide + H2O
Glu-Ala-Ala-Phe + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
?
glutaminase C + H2O
?
show the reaction diagram
when misfolded or unfolded
-
-
?
Mgm101 + H2O
?
show the reaction diagram
a yeast mitochondrial protein. The substrate is protected from degradation when bound to a nucleic acid
-
-
?
mitochondrial aconitase + H2O
?
show the reaction diagram
when misfolded or unfolded
-
-
?
mitochondrial transcription factor A + H2O
?
show the reaction diagram
i.e. TFAM
-
-
?
MrpL32 + H2O
?
show the reaction diagram
steroidogenic acute regulatory protein + H2O
?
show the reaction diagram
-
-
-
?
TFAM + H2O
?
show the reaction diagram
Twinkle helicase + H2O
?
show the reaction diagram
acyl-CoA oxidase + H2O
?
show the reaction diagram
-
exhibits little, if any, in vitro acyl-CoA oxidase processing activity
-
-
?
alpha-casein + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
phosphate + ADP
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
ATP dependent degradation>
-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
alpha-casein
-
-
?
Cox4-1 + H2O
?
show the reaction diagram
-
-
-
-
?
DNA
?
show the reaction diagram
-
mitochondrial lon binds preferentially to single-stranded DNA in a sequence-dependent manner
-
-
?
FITC casein + H2O
?
show the reaction diagram
-
-
-
-
?
FITC-casein + H2O
?
show the reaction diagram
-
-
-
-
?
FRETN 89-98Abu + H2O
?
show the reaction diagram
-
peptide-based substrate containing the Y(NO2)-Abz internal fluorescence quenching pair and peptide sequence RGIT-Abu-SGRQK, no substrate for human protease ClpXP
-
-
?
hydroxyacyl-coenzyme A dehydrogenase + H2O
?
show the reaction diagram
-
-
-
-
?
lambda phage DNA + H2O
?
show the reaction diagram
-
-
-
?
lambda phage N protein + H2O
?
show the reaction diagram
-
-
-
-
?
mitochondrial aconitase + H2O
?
show the reaction diagram
-
essential enzyme, particularly susceptible to oxidative damage, preferentially oxidatively modified and inactivated during ageing
-
?
mitochondrial processing peptidase alpha subunit + H2O
?
show the reaction diagram
MPPalpha + H2O
?
show the reaction diagram
-
mitochondrial processing peptidase alpha-subunit (MPPalpha), to show that mitochondrial Lon also degrades folded proteins and initiates substrate cleavage non-processively. Two mitochondrial substrates with known or homology-derived three-dimensional structures are used
-
-
?
native aconitase + H2O
?
show the reaction diagram
-
degradation at a lower efficiency than oxidized aconitase
-
-
?
oxidized aconitase + H2O
?
show the reaction diagram
-
oxidatively modified proteins and unfolded peptides are good substrates for proteolysis by lon
-
-
?
PMP70 + H2O
?
show the reaction diagram
-
-
-
-
?
polymerase gamma + H2O
?
show the reaction diagram
-
-
-
-
?
PTS1 protein + H2O
?
show the reaction diagram
-
-
-
-
?
RNA
?
show the reaction diagram
-
mitochondrial lon binds preferentially to single-stranded RNA in a sequence-dependent manner
-
-
?
StAR + H2O
?
show the reaction diagram
-
steroidogenic acute regulatory protein (StAR), to show that mitochondrial Lon also degrades folded proteins and initiates substrate cleavage non-processively. Two mitochondrial substrates with known or homology-derived three-dimensional structures are used
-
-
?
steroidogenic acute regulatory protein + H2O
?
show the reaction diagram
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
show the reaction diagram
-
-
-
?
Y(3-NO2)-RGITCSGRQ-K(anthranilamide) + H2O
Y(3-NO2)-RGITC + SGRQ-K(anthranilamide)
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-aminolevulinic acid synthase + H2O
?
show the reaction diagram
-
-
-
?
cystathionine beta-synthase + H2O
?
show the reaction diagram
when misfolded or unfolded
-
-
?
cytochrome c oxidase 4 isoform 1 + H2O
?
show the reaction diagram
i.e. COX4-1
-
-
?
glutaminase C + H2O
?
show the reaction diagram
when misfolded or unfolded
-
-
?
mitochondrial aconitase + H2O
?
show the reaction diagram
when misfolded or unfolded
-
-
?
mitochondrial transcription factor A + H2O
?
show the reaction diagram
i.e. TFAM
-
-
?
MrpL32 + H2O
?
show the reaction diagram
human MrpL32, a component of the 39S large subunit of the mitochondrial ribosome
-
-
?
steroidogenic acute regulatory protein + H2O
?
show the reaction diagram
-
-
-
?
TFAM + H2O
?
show the reaction diagram
only DNA-free TFAM is a substrate for human mitochondrial Lon. TFAM is released from DNA upon phosphorylation by protein kinase A, and TFAM not bound to DNA, whether phosphorylated or not, is a substrate for the ATP-dependent mitochondrial Lon protease
-
-
?
Twinkle helicase + H2O
?
show the reaction diagram
a human mitochondrial protein
-
-
?
mitochondrial aconitase + H2O
?
show the reaction diagram
-
essential enzyme, particularly susceptible to oxidative damage, preferentially oxidatively modified and inactivated during ageing
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
stabilizes the enzyme complex
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
anti-sense morpholino oligonucleotide
-
causes defects in mitochondrial membrane potential, respiration and morphology, as well as apoptotic cell death
-
clasto-lactacystin beta-lactone
-
blocks lon-mediated degradation of steroidogenic acute regulatory protein or FITC casein
dansyl-YRGIT-Abu-B(OH)2
-
i.e. DBN93, site-directed peptide inhibitor with two-step mechanism
H2O2
-
blocks enzymatic activity but has no appreciable effect on sequence-specific binding to DNA. 0.1 mM decreases proteolytic activity to ca. 60%, at 0.5, 1, and 4 mM protease activity is reduced to 18, 9, and 5%, respectively
MG132
-
blocks lon-mediated degradation of steroidogenic acute regulatory protein or FITC casein
MG262
-
-
RNAi
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
human mitochondrial lon degrades mouse StAR in the presence of ATP, but not in its absence
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.027
FRETN 89-98
pH 8.0, 37°C, recombinant enzyme
1.3
Y(3-NO2)-RGITCysSGRQ-K(anthranilamide)
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.63
FRETN 89-98
pH 8.0, 37°C, recombinant enzyme
5.9
Y(3-NO2)-RGITCysSGRQ-K(anthranilamide)
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.46
FRETN 89-98
pH 8.0, 37°C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.79
ADP
pH 8.0, 37°C, recombinant enzyme
0.000021 - 0.00135
dansyl-YRGIT-Abu-B(OH)2
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
clasto-lactacystin beta-lactone
Homo sapiens
-
-
0.02
MG132
Homo sapiens
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
wild-type and HtrA2 knock-down HEK293T cells
Manually annotated by BRENDA team
hippocampus, human
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cells overexpressing lon contain large peroxisomes, but number of peroxisomes in these cells are less than that in wild-type cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
functions of Lon protease in human mitochondria, overview. Lon expression highly correlates with expression of heat shock 60 kDa protein-1 (HSPD1), heat shock 10 kDa protein-1 (HSPE1), heat shock 70 kDa protein-9 (HSPA9), and caseinolytic mitochondrial matrix peptidase proteolytic subunit (CLPP), which are all involved in the mitochondrial unfolded protein response (UPRmt)
physiological function
evolution
-
the enzyme is a member of the ATPase superfamily
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LONM_HUMAN
959
0
106489
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
Western blotting
106000
calculated from cDNA
100000
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
heptamer
-
cryoelectron microscopy
hexamer or heptamer
-
stabilized by Mg2+ and ADP bound to the ATPase region
oligomer
-
6-7 * 100000, homo-oligomeric complex, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
human Lon is target of deacetylase sirtuin 3 (SIRT3), likely at Lys917, which is near the catalytic dyad, thus suggesting that Lon proteolytic activity can be regulated via deacetylation
acetylation
-
acetylation of residue K917, located on the surface of the catalytic domain. Sirtuin 3 interacts with Lon protease and regulates its acetylation status, protein-protein docking analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme mutant S855A in complex with non-hydrolyzable ATP analogue AMP-PNP and with ADP, X-ray diffraction structure determination and analysis at resolutions of 15 A and 21 A, respectively, fitting of X-rays structures and cryo-electron microscopy structures, overview
structure of the proteolytic domain of human mitochondrial Lon at 2 A resolution. There are six protomers in the asymmetric unit, four arranged as two dimers. The intersubunit interactions within the two dimers are similar to those between adjacent subunits of the hexameric ring of Escherichia coli Lon. The active site contains a 310 helix attached to the N-terminal end of alpha-helix 2, which leads to the insertion of Asp852 into the active site. Structural considerations make it likely that this conformation is proteolytically inactive. A mechanism relating the formation of Lon oligomers with a conformational shift in the active site region coupled to a movement of a loop in the oligomer interface may convert the proteolytically inactive form seen here to the active one in the Escherichia coli hexamer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S855A
delta75-490
-
dominant negative mutant, exhibits a remarkable decrease in acyl-CoA oxidase and mislocalization of catalase to the cytoplasm. Shows lower beta-oxidation activity than wild-type
G893A
-
site-directed mutagenesis, the mutant shows 63% of wild-type ATPase activity, 80% of wild-type protease activity, and 2.27fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894A
-
site-directed mutagenesis, the mutant shows 103% of wild-type ATPase activity, 79% of wild-type protease activity, and 0.745fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894P
-
site-directed mutagenesis, the mutant shows 112% of wild-type ATPase activity, no protease activity, and 0.32fold of the activation by beta-casein compared to the wild-type enzyme
G893P
-
site-directed mutagenesis, the mutant shows 89% of wild-type ATPase activity, no protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G893P/G894A
-
site-directed mutagenesis, the mutant shows 71% of wild-type ATPase activity, 8% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894A
-
site-directed mutagenesis, the mutant shows 139% of wild-type ATPase activity, 76% of wild-type protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G894P
-
site-directed mutagenesis, the mutant shows 130% of wild-type ATPase activity, 84% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894S
-
site-directed mutagenesis, the mutant shows 140% of wild-type ATPase activity, 47% of wild-type protease activity, and 0.88fold of the activation by beta-casein compared to the wild-type enzyme
K529R
-
site-directed mutagenesis, inactive mutant
S743A
-
point mutant at the center of the protease catalytic domain
S855A
S885A
-
site-directed mutagenesis, three-dimensional structure of the ADP-bound Lon S885A mutant obtained by electron microscopy as a result of preliminary negative staining studies
T880V
-
site-directed mutagenesis, the mutant shows 46% of wild-type ATPase activity, 107% of wild-type protease activity, and 3.28fold of the activation by beta-casein compared to the wild-type enzyme
W770A
-
site-directed mutagenesis, the mutant shows 98.5% of wild-type ATPase activity, 6.4% of wild-type protease activity, and 0.305fold of the activation by beta-casein compared to the wild-type enzyme
W770P
-
site-directed mutagenesis, the mutant shows 123% of wild-type ATPase activity, 55.3% of wild-type protease activity, and 0.64fold of the activation by beta-casein compared to the wild-type enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
hLon ist rapidly digested by trypsin, ADP binding does not protect
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain Rosetta (DE3) by ultrafiltration and gel filtration
by gel filtration, to near homogeneity
-
gel filtration
-
human lon is overproduced and purified from the Rosetta Escherichia coli strain. Human mitochondrial lon degrades mouse StAR in the presence of ATP, but not in its absence
-
on Ni2+-NTA column
-
recombinant enzyme
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by ultracentrifugation, nickel affinity chromatography and gel filtration
-
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the proteolytic domain, residues 741-959, in Escherichia coli
gene Lonp1
gene LONP1, recombinant expression of the enzyme in Escherichia coli strain Rosetta (DE3)
cDNA clone pHHCPK77, 51 kDa fragment expressed in Escherichia coli BL21(DE3)
cDNAcloned and expressed in Escherichia coli Rosetta strain
-
expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta 2 (DE3)
-
gene Lonp1
-
into the NdeI and BamHI sites of proEX, lon (proEX-Lon-His) expressed in Escherichia coli. Plasmid lon O/Ex expressed in COS cells
-
NdeI-BamHI fragment from proEx-1/lon cloned into pET24c(+), overexpressed in Escherichia coli Rosetta (DE3)
-
recombinant expression of His-tagged wild-type and mutant enzyme in Escherichia coli
-
recombinant lon expressed in COS-7 cells. HEK293 cell lines stably expressing wild-type lon and its internal deletion mutant delta75-490, by using the retrovirus expression system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Lon is upregulated after serum starvation
modest induction of mRNA after H2O2 treatment, with the highest inductions of 2.3fold at 4 h and 1.7fold at 7 h observed when the cells are treated with 0.100 mM H2O2 and 1.9fold at 4 h and 1.6fold at 7 h after 0.200 mM H2O2 treatment. Cells exposed to a 45°C heat shock exhibit an 80% induction of Lon protein after 1 h of shock, and 31% induction after 3 h recovery, gradually returning to basal levels at 6 and 24 h. Lon up-regulation by heat-shock is accompanied by a coinduction of mtHSP-70, which exhibits a 70% increase after 1 h of heat shock and declines to basal levels thereafter. Serum starvation stress for 1 h does not increase Lon levels. After recovery for 3 h in serum-supplemented medium, Lon protein levels exhibit a 4-fold increase. Lon protein levels after 6 and 24 h of serum starvation stress recovery remains relatively high, with protein inductions of about 3.8- and 3.1fold, respectively
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
high levels of LONP1 are a poor prognosis marker in human colorectal cancer and melanoma
medicine
-
lon and aconitase may be key players in the maintenance of mitochondrial homeostasis under conditions of stress, partial compromise of their function may contribute to both aging and degenerative diseases
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, N.; Gottesman, S.; Willingham, M.C.; Gottesman, M.M.; Maurizi, M.R.
A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease
Proc. Natl. Acad. Sci. USA
90
11247-11251
1993
Brevibacillus brevis, Escherichia coli, Homo sapiens, Homo sapiens (P36776), Myxococcus xanthus
Manually annotated by BRENDA team
Lu, B.; Liu, T.; Crosby, J.A.; Thomas-Wohlever, J.; Lee, I.; Suzuki, C.K.
The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals
Gene
306
45-55
2003
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Botos, I.; Melnikov, E.E.; Cherry, S.; Tropea, J.E.; Khalatova, A.G.; Rasulova, F.; Dauter, Z.; Maurizi, M.R.; Rotanova, T.V.; Wlodawer, A.; Gustchina, A.
The catalytic domain of E.coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
J. Biol. Chem.
279
8140-8148
2003
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Bota, D.A.; Davies, K.J.
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
Nat. Cell Biol.
4
674-680
2002
Homo sapiens
Manually annotated by BRENDA team
Liu, T.; Lu, B.; Lee, I.; Ondrovicova, G.; Kutejova, E.; Suzuki, C.K.
DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrates
J. Biol. Chem.
279
13902-13910
2004
Homo sapiens
Manually annotated by BRENDA team
Ondrovicova, G.; Liu, T.; Singh, K.; Tian, B.; Li, H.; Gakh, O.; Perecko, D.; Janata, J.; Granot, Z.; Orly, J.; Kutejova, E.; Suzuki, C.K.
Cleavage site selection within a folded substrate by the ATP-dependent Lon protease
J. Biol. Chem.
280
25103-25110
2005
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Ngo, J.K.; Davies, K.J.
Importance of the lon protease in mitochondrial maintenance and the significance of declining lon in aging
Ann. N. Y. Acad. Sci.
1119
78-87
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Frase, H.; Hudak, J.; Lee, I.
Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease
Biochemistry
45
8264-8274
2006
Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Lee, I.; Suzuki, C.K.
Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates
Biochim. Biophys. Acta
1784
727-735
2008
Saccharomyces cerevisiae, Brucella abortus, Caulobacter vibrioides, Escherichia coli, Homo sapiens, Mycolicibacterium smegmatis, Pseudomonas aeruginosa, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Thermoplasma acidophilum
Manually annotated by BRENDA team
Omi, S.; Nakata, R.; Okamura-Ikeda, K.; Konishi, H.; Taniguchi, H.
Contribution of peroxisome-specific isoform of Lon protease in sorting PTS1 proteins to peroxisomes
J. Biochem.
143
649-660
2008
Homo sapiens
Manually annotated by BRENDA team
Lu, B.; Yadav, S.; Shah, P.G.; Liu, T.; Tian, B.; Pukszta, S.; Villaluna, N.; Kutejova, E.; Newlon, C.S.; Santos, J.H.; Suzuki, C.K.
Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance
J. Biol. Chem.
282
17363-17374
2007
Homo sapiens
Manually annotated by BRENDA team
Lee, I.; Berdis, A.J.; Suzuki, C.K.
Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies
Mol. Biosyst.
2
477-483
2006
Saccharomyces cerevisiae, Brucella abortus, Escherichia coli, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Granot, Z.; Kobiler, O.; Melamed-Book, N.; Eimerl, S.; Bahat, A.; Lu, B.; Braun, S.; Maurizi, M.R.; Suzuki, C.K.; Oppenheim, A.B.; Orly, J.
Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors
Mol. Endocrinol.
21
2164-2177
2007
Homo sapiens
Manually annotated by BRENDA team
Tsilibaris, V.; Maenhaut-Michel, G.; Van Melderen, L.
Biological roles of the Lon ATP-dependent protease
Res. Microbiol.
157
701-713
2006
Brevibacillus brevis, Bacillus subtilis, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Homo sapiens, Myxococcus xanthus, no activity in Lactobacillus sp., no activity in Streptococcus sp., Yersinia pestis, Proteus mirabilis, Pseudomonas syringae, Salmonella enterica subsp. enterica serovar Typhimurium, Streptomyces lividans, Vibrio parahaemolyticus, no activity in Mycobacterium tuberculosis, no activity in Mycobacterium leprae
Manually annotated by BRENDA team
Chen, S.H.; Suzuki, C.K.; Wu, S.H.
Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA
Nucleic Acids Res.
36
1273-1287
2008
Homo sapiens
Manually annotated by BRENDA team
Ngo, J.K.; Davies, K.J.
Mitochondrial Lon protease is a human stress protein
Free Radic. Biol. Med.
46
1042-1048
2009
Homo sapiens
Manually annotated by BRENDA team
Garcia-Nafria, J.; Ondrovicova, G.; Blagova, E.; Levdikov, V.M.; Bauer, J.A.; Suzuki, C.K.; Kutejova, E.; Wilkinson, A.J.; Wilson, K.S.
Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity
Protein Sci.
19
987-999
2010
Homo sapiens (P36776), Homo sapiens
Manually annotated by BRENDA team
Fishovitz, J.; Li, M.; Frase, H.; Hudak, J.; Craig, S.; Ko, K.; Berdis, A.J.; Suzuki, C.K.; Lee, I.
Active-site-directed chemical tools for profiling mitochondrial Lon protease
ACS Chem. Biol.
6
781-788
2011
Homo sapiens
Manually annotated by BRENDA team
Quiros, P.M.; Espanol, Y.; Acin-Perez, R.; Rodriguez, F.; Barcena, C.; Watanabe, K.; Calvo, E.; Loureiro, M.; Fernandez-Garcia, M.S.; Fueyo, A.; Vazquez, J.; Enriquez, J.A.; Lopez-Otin, C.
ATP-dependent Lon protease controls tumor bioenergetics by reprogramming mitochondrial activity
Cell Rep.
8
542-556
2014
Homo sapiens, Mus musculus (Q8CGK3)
Manually annotated by BRENDA team
Goo, H.G.; Rhim, H.; Kang, S.
HtrA2/Omi influences the stability of LON protease 1 and prohibitin, proteins involved in mitochondrial homeostasis
Exp. Cell Res.
328
456-465
2014
Homo sapiens (P36776), Mus musculus (Q8CGK3), Mus musculus
Manually annotated by BRENDA team
Ambro, L.; Pevala, V.; Ondrovicova, G.; Bellova, J.; Kunova, N.; Kutejova, E.; Bauer, J.
Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities
FEBS J.
281
1784-1797
2014
Homo sapiens
Manually annotated by BRENDA team
Kereiche, S.; Kovacik, L.; Pevala, V.; Ambro, L.; Bellova, J.; Kutejova, E.; Raska, I.
Three-dimensional reconstruction of the S885A mutant of human mitochondrial Lon protease
Folia Biol. (Praha)
60 Suppl 1
62-65
2014
Homo sapiens
Manually annotated by BRENDA team
Gibellini, L.; Pinti, M.; Beretti, F.; Pierri, C.L.; Onofrio, A.; Riccio, M.; Carnevale, G.; De Biasi, S.; Nasi, M.; Torelli, F.; Boraldi, F.; De Pol, A.; Cossarizza, A.
Sirtuin 3 interacts with Lon protease and regulates its acetylation status
Mitochondrion
18
76-81
2014
Homo sapiens
Manually annotated by BRENDA team
Pinti, M.; Gibellini, L.; Nasi, M.; De Biasi, S.; Bortolotti, C.A.; Iannone, A.; Cossarizza, A.
Emerging role of Lon protease as a master regulator of mitochondrial functions
Biochim. Biophys. Acta
1857
1300-1306
2016
Thermococcus onnurineus (B6YU74), Escherichia coli (P0A9M0), Saccharomyces cerevisiae (P36775), Homo sapiens (P36776), Mus musculus (Q8CGK3), Saccharomyces cerevisiae ATCC 204508 (P36775)
Manually annotated by BRENDA team
Fishovitz, J.; Sha, Z.; Chilakala, S.; Cheng, I.; Xu, Y.; Lee, I.
Utilization of mechanistic enzymology to evaluate the significance of ADP binding to human Lon protease
Front. Mol. Biosci.
4
47
2017
Escherichia coli (P0A9M0), Escherichia coli, Homo sapiens (P36776), Homo sapiens
Manually annotated by BRENDA team
Kereiche, S.; Kovacik, L.; Bednar, J.; Pevala, V.; Kunova, N.; Ondrovicova, G.; Bauer, J.; Ambro, L.; Bellova, J.; Kutejova, E.; Raska, I.
The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease
Sci. Rep.
6
33631
2016
Homo sapiens (P36776), Homo sapiens
Manually annotated by BRENDA team
Kunova, N.; Ondrovicova, G.; Bauer, J.A.; Bellova, J.; Ambro, L.; Martinakova, L.; Kotrasova, V.; Kutejova, E.; Pevala, V.
The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
Sci. Rep.
7
631
2017
Saccharomyces cerevisiae (P36775), Saccharomyces cerevisiae, Homo sapiens (P36776), Homo sapiens, Saccharomyces cerevisiae ATCC 204508 (P36775)
Manually annotated by BRENDA team