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Enzyme Nomenclature
Information on EC 3.4.21.53 - Endopeptidase La
for references in articles please use BRENDA:EC3.4.21.53
Word Map on EC 3.4.21.53
- 3.4.21.53
- trypsin
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antiretroviral
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immunodeficiency
- inflammatory
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cathepsins
- plasminogen
-
hiv-infected
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antiviral
- coagulation
- thrombin
- inflammation
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elastase
- nucleoside
-
virological
- injury
- neutrophil
- glycoprotein
- pancreatic
- endothelial
- viruses
- chymotrypsin
- lymphocyte
- lysosomal
- plasmin
- alzheimer
- leukocyte
- collagen
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calpains
-
caspase
- proteasome
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pharmacokinetic
-
amyloid
- platelet
- heparin
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kallikreins
- clot
-
anticoagulant
- urokinase
-
amylase
- upa
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fibrinogen
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metalloproteinases
- fibrin
- papain
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fibrinolytic
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thrombotic
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urokinase-type
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antithrombin
-
zymography
-
tissue-type
- diagnostics
- medicine
- biotechnology
- agriculture
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.21.53
-
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RECOMMENDED NAME
GeneOntology No.
Endopeptidase La
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins in presence of ATP
hydrolysis of proteins in presence of ATP, mechanism
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hydrolysis of proteins in presence of ATP
hydrolysis of proteins in presence of ATP, mechanism
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hydrolysis of proteins in presence of ATP
hydrolysis of proteins in presence of ATP, mechanism
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hydrolysis of proteins in presence of ATP
hydrolysis of proteins in presence of ATP, mechanism
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hydrolysis of proteins in presence of ATP
hydrolysis of proteins in presence of ATP, mechanism
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hydrolysis of proteins in presence of ATP
hydrolysis of proteins in presence of ATP, mechanism
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hydrolysis of proteins in presence of ATP
binding of ATP induces a conformational change that facilitates the coupling of nucleotide hydrolysis with peptide substrate delivery to the peptidase activs site
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hydrolysis of proteins in presence of ATP
pre-steady state kinetic characterization. ATP hydrolysis occurs before peptide cleavage, with the former displaying a burst and the latter displaying a lag in the product production. ATP hydrolysis is used to generate an active enzyme that hydrolyzes peptide
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hydrolysis of proteins in presence of ATP
active site contains a Ser-Lys dyad
hydrolysis of proteins in presence of ATP
presence of a catalytic Ser-Lys dyad. Definition of two enzyme subfamilies LonA and LonB, based on the consensus sequences in the active site of the proteolytic domain
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hydrolysis of proteins in presence of ATP
active site consists of catalytic Ser-Lys-Asp residues. Charged Lys-593 assists in lowering the pKa of the Ser550 hydroxyl group, and the water in the cavity acts as a proton acceptor during catalysis
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hydrolysis of proteins in presence of ATP
reaction may involve a substrate translocation step limiting the turnover rate
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hydrolysis of proteins in presence of ATP
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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linked with ATP hydrolysis
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CAS REGISTRY NUMBER
COMMENTARY
79818-35-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
IBDVP2, strain P2, two-segmented double-stranded RNA virus
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gene is part of an operon that encodes membrane proteases and is transcribed as a polycistronic mRNA in cells at different growth stages
UniProt
gene is part of an operon that encodes membrane proteases and is transcribed as a polycistronic mRNA in cells at different growth stages
UniProt
formerly Pseudomonas fluorescens, gene PFL_3985
UniProt
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expression is heat-inducible. In addition to ATPase activity and peptidase activity, enzyme has an ATP-independent chaperone-like activity
Q84FG5
SwissProt
expression is heat-inducible. In addition to ATPase activity and peptidase activity, enzyme has an ATP-independent chaperone-like activity
Q84FG5
SwissProt
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29339, 29342, 29344, 29345, 29346, 29347, 29348, 29351, 29352, 29353, 29354, 29356, 29357, 29360, 29361, 29362, 649538, 649846, 650178, 651134, 651238, 651245, 651310, 651419, 651641, 651835, 651853, 651873, 651911, 653631, 667610, 667645, 668465, 668624, 669248, 669554, 670039, 670225, 670304, 670826, 670878, 677923, 678145, 678185, 678244, 678475, 678789, 681850, 682726, 682821, 695302, 696457, 698108, 699582, 700273, 707165, 707168, 707377, 707411, 707752, 709125, 709998, 710416, 717743, 718132, 731814, 732532, 732825, 732882, 732906
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29357, 669354, 677574, 678206, 678475, 680569, 680779, 681850, 681937, 682821, 700494, 708563, 717017, 731797, 731835, 732469
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; enzyme immunochemically related with Escherichia coli protease la; yeast, mutant strain pep949
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
although Lon is originally identified as an ATP-dependent protease with fused AAA+ (ATPases associated with diverse cellular activities) and protease domains, analyses have recently identified LonC as a class of Lon-like proteases with no intrinsic ATPase activity. In contrast to the canonical ATP-dependent Lon present in eukaryotic organelles and prokaryotes, LonC contains an AAA-like domain that lacks the conserved ATPase motifs
evolution
the enzyme is a member of the ATP-dependent protease family
evolution
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evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases, Escherichia coli utilizes five different AAA+ proteases: Lon, ClpXP, ClpAP, HslUV, and FtsH
evolution
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homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins
evolution
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the enzyme is a member of the ATP-dependent protease family
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malfunction
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Hvlon can be deleted from the chromosome only when a copy of the wild type gene is provided in trans suggesting that Lon is essential for survival in this archaeon. The contents of bacterioruberins and some polar lipids were increased in the lon mutants suggesting that Lon is linked to maintenance of membrane lipid balance which likely affects cell viability in this archaeon
malfunction
the stem nodules in the host legume Sesbania rostrata formed by the lon mutant show little or no nitrogen fixation activity. The reb genes are highly expressed in the lon mutant, high expression of reb genes in part causes aberrance in the Azorhizobium caulinodans-Sesbania rostrata symbiosis
malfunction
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overexpression of the enzyme increases tumorigenesis, high levels of LONP1 are a poor prognosis marker in human colorectal cancer and melanoma, phenotypes, overview
malfunction
homozygous deletion of Lonp1 causes early embryonic lethality, whereas its haploinsufficiency protects against colorectal and skin tumors. LONP1 knockdown inhibits cellular proliferation and tumor and metastasis formation, phenotypes, overview. LONP1 is necessary for proliferation and metastasis of melanoma cells
malfunction
in a lon mutant, the steady-state levels and the stability of the GacA protein are significantly elevated at the end of exponential growth, the expression of the sRNAs RsmY and RsmZ and that of dependent physiological functions such as antibiotic production are significantly enhanced. In starved cells, the loss of Lon function prolonged the half-life of the GacA protein. The lon mutant has a higher biocontrol activity per viable cell, but this positive effect appears to be compromised by a reduced fitness of the mutant in the rhizosphere on cucumber. Biocontrol of Pythium ultimum on cucumber roots requires fewer lon mutant cells than wild-type cells. In starved cells, the loss of Lon function prolonges the half-life of the GacA protein. The lon mutant exhibits increased aprA expression and antibiotic activity
malfunction
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altered expression levels of the enzyme are linked to some severe diseases such as epilepsy, myopathy, or lateral sclerosis
malfunction
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lon mutants are supersusceptible to ciprofloxacin, and exhibit a defect in cell division and in virulence-related properties, such as swarming, twitching and biofilm formation, despite the fact that the Lon protease is not a traditional regulator. The lon mutant has a defect in cytotoxicity towards epithelial cells, is less virulent in an amoeba model as well as a mouse acute lung infection model, and is impacted on in vivo survival in a rat model of chronic infection. The lon mutation leads to a downregulation of Type III secretion genes. The Lon protease also influenced motility and biofilm formation in a mucin-rich environment, defective virulence in vivo. Phenotype detailed overview
malfunction
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the stem nodules in the host legume Sesbania rostrata formed by the lon mutant show little or no nitrogen fixation activity. The reb genes are highly expressed in the lon mutant, high expression of reb genes in part causes aberrance in the Azorhizobium caulinodans-Sesbania rostrata symbiosis
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malfunction
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in a lon mutant, the steady-state levels and the stability of the GacA protein are significantly elevated at the end of exponential growth, the expression of the sRNAs RsmY and RsmZ and that of dependent physiological functions such as antibiotic production are significantly enhanced. In starved cells, the loss of Lon function prolonged the half-life of the GacA protein. The lon mutant has a higher biocontrol activity per viable cell, but this positive effect appears to be compromised by a reduced fitness of the mutant in the rhizosphere on cucumber. Biocontrol of Pythium ultimum on cucumber roots requires fewer lon mutant cells than wild-type cells. In starved cells, the loss of Lon function prolonges the half-life of the GacA protein. The lon mutant exhibits increased aprA expression and antibiotic activity
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metabolism
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mitochondrial calpain 10 is selectively degraded by Lon protease under basal conditions and is enhanced under and oxidizing conditions, while cytosolic calpain 10 is degraded by the proteasome
metabolism
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the enzyme has a global impact on the physiology of the euryarchaeon Haloferax volcanii, affecting key cellular processes as well as organism-specific so far unknown functions which may be required for survival/adaptation under extreme conditions
metabolism
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plant mitochondrial protein carbonylation, an irreversible oxidative protein modification that inactivates the protein function, and role of the ATP-dependent proteases in defending mitochondria against accumulation of carbonylated proteins, overview. In plants, carbonylated proteins are found in virtually all cellular compartments - cytosol, chloroplasts, peroxisomes, nucleus, and mitochondria - and in the entire plant life cycle with especially high levels at certain stages of growth and development. Carbonylated breakdown products of mitochondrial proteins might act as secondary messengers in retrograde signaling from plant mitochondria to the nucleus. mitochondria depend on a series of pathways that continuously monitor and remove oxidatively damaged proteins
metabolism
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the enzyme has a global impact on the physiology of the euryarchaeon Haloferax volcanii, affecting key cellular processes as well as organism-specific so far unknown functions which may be required for survival/adaptation under extreme conditions
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metabolism
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mitochondrial calpain 10 is selectively degraded by Lon protease under basal conditions and is enhanced under and oxidizing conditions, while cytosolic calpain 10 is degraded by the proteasome
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physiological function
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absence of Lon protease blocks paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocks a parallel increase in cell lysate viscosity likely to reflect DNA size
physiological function
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transposon inactivation of ycgE, encoding a putative transcriptional regulator, leads to decreased multidrug susceptibility in an Escherichia coli lon mutant. The multidrug susceptibility phenotype e.g., to tetracycline and beta-lactam antibiotics, requires the inactivation of both lon and ycgE. In this mutant, a decreased amount of OmpF porin contributes to the lowered drug susceptibility, with a greater effect at 26°C than at 37°C
physiological function
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the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
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the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
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the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
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Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible
physiological function
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the Lon protease is a stress-responsive protein that is induced by multiple stressors, including heat shock, serum starvation, and oxidative stress. Lon induction, by pretreatment with low-level stress, protects against oxidative protein damage, diminished mitochondrial function, and loss of cell proliferation induced by toxic levels of hydrogen peroxide. Blocking Lon induction with Lon siRNA also blocks this induced protection
physiological function
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Pim1-mediated proteolysis is required for elimination of oxidatively damaged proteins in mitochondria. Pim1 plays a prevalent role in mitochondrial protein quality control
physiological function
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the Lon protease and the SecB and DnaJ/Hsp40 chaperones are involved in the quality control of presecretory proteins in Escherichia coli. Mutations in the lon gene alleviate the cold-sensitive phenotype of a secB mutant. In comparison to the respective single mutants, the double secB lon mutant strongly accumulates aggregates of SecB substrates at physiological temperatures, suggesting that the chaperone and the protease share substrates. The main substrates identified in secB lon aggregates, namely proOmpF and proOmpC, are highly sensitive to specific degradation by Lon. In contrast, both substrates are significantly protected from Lon degradation by SecB. The chaperone DnaJ by itself protects substrates better from Lon degradation than SecB or the complete DnaK/DnaJ/GrpE chaperone machinery
physiological function
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deletion of genes cpxR and lon results in mutants highly similar to wild-type. In comparison with the wild-type, 1.5- to 3.3fold increases of fimbrial products such as Agf, Fim, and Pef fimbria are observed in the single and double mutants. lon single and cpxR and lon double mutants morphologically appear elongated in shape and produce 2.0- and 3.2fold increases, respectively, of capsular polysaccharide, which is a major antigenic component. Approximately 104fold attenuation assessed by analysis of LD50 of BALB/c mouse is observed by deleting the lon/cpxR genes
physiological function
a lon2 disruption mutant is mildly resistant to the inhibitory effects of indole-3-butyric acid on root elongation, resistant to the stimulatory effects of indole-3-butyric acid on lateral root production and display succinate dependence during seedling growth. lon2 mutants display defects in removing the type 2 peroxisome targeting signal PTS2 from peroxisomal malate dehydrogenase and reduced accumulation of 3-ketoacyl-CoA thiolase, another PTS2-containing protein, both defects are not apparent upon germination but appear in 5 to 8 days old seedlings. In lon2 cotyledon cells, matrix proteins are localized to peroxisomes in 4 days old seedlings but mislocalized to the cytosol in 8 days old seedlings. A PTS2-green fluorescent protein reporter sorts to peroxisomes in lon2 root tip cells but is largely cytosolic in more mature root cells. LON2 is needed for sustained matrix protein import into peroxisomes
physiological function
Lon-1 may be important in host adaptation from the arthropod to a warm-blooded host. Recombinant Lon-1 shows properties of an ATP-dependent chaperone protease in vitro but does not complement an Escherichia coli Lon mutant; Lon-2 is engaged in cellular homeostasis
physiological function
purified Lon binds double stranded as well as single stranded DNA in the presence of elevated salt concentrations
physiological function
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mitochondrial proteins aggregate to a substantial extent if they are challenged by either heat stress or reactive oxygen. As an important aspect of quality control, the proteolytic activity of Pim1 prevents the accumulation of these aggregation-prone polypeptides, resulting in prevention of proteotoxic effects
physiological function
Q52MC0;
lon disruption mutants show increased UV sensitivity, and produce higher levels of tabtoxin than the wild-type. Strains with lon disruption elicit the host defense system more rapidly and strongly than the wild-type strain, suggesting that the Lon protease is essential for systemic pathogenesis
physiological function
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reduction of Lon to less than 10% of its normal level in Drosophila Schneider cells by RNAi knockdown results in increased abundance of mitochondrial transcription factor A, TFAM, and mitochondrial DNA copy number. In a corollary manner, overexpression of Lon reduces TFAM levels and mt DNA copy number. Induction of mitochondrial DNA depletion in Lon knockdown cells does not result in degradation of TFAM, thereby causing a dramatic increase in the TFAM:mitochondrial DNA ratio. The increased TFAM:mitochondrial DNA ratio in turn causes inhibition of mitochondrial transcription
physiological function
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the enzyme controls membrane lipids composition and is essential for viability in the extremophilic haloarchaeon Haloferax volcanii
physiological function
the Lon-insertion domain of LonC is involved both in Skplike chaperone activity and in recognition of unfolded protein substrates, structure of Lon-insertion domain is remarkably similar to the tentacle-like prong of the periplasmic chaperone Skp
physiological function
Lon protease is required to suppress the expression of the reb genes. Lon protease is also involved in the regulation of exopolysaccharide production and autoagglutination of bacterial cells
physiological function
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the enzyme plays a key role in metabolic reprogramming by remodeling OXPHOS complexes and protecting against senescence. The protease is a central regulator of mitochondrial activity in oncogenesis. LONP1 is necessary for proliferation and metastasis of melanoma cells
physiological function
the enzyme plays a key role in metabolic reprogramming by remodeling OXPHOS complexes and protecting against senescence. The protease is a central regulator of mitochondrial activity in oncogenesis. Role of LONP1 in the regulation of mitochondrial function in cancer, overview
physiological function
ATP-dependent proteases, e.g. represented by Lon, are stress proteins that are induced in bacterial cells in response to unfavourable conditions. The enzyme negatively affects GacA protein stability and expression of the Gac/Rsm signal transduction pathway in Pseudomonas protegens, it is an important negative regulator of the Gac/Rsm signal transduction pathway in the organism. The Gac/Rsm signal transduction pathway controls secondary metabolism and suppression of fungal root pathogens via the expression of regulatory small RNAs, overview
physiological function
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the enzyme expression in reguated by HtrA2 serine protease, Lon1 protease is overexpressed in HtrA2-deficient cells, phenotype, overview. HtrA2 regulates mitochondrial proteins through its serine protease activity
physiological function
the enzyme expression in reguated by HtrA2 serine protease, Lon1 protease is overexpressed in HtrA2-deficient cells, phenotype, overview. HtrA2 regulates mitochondrial proteins through its serine protease activity
physiological function
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protease Lon eliminates an immature or misfolded molybdoenzyme probably by targeting its inactive catalytic site, it is involved in the apoTorA degradation process
physiological function
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the main function of the enzyme is the control of protein quality and the maintenance of proteostasis by degradation of misfolded and damaged proteins, which occur in response to numerous stress conditions. It also participates in the regulation of levels of transcription factors that control pathogenesis, development and stress response
physiological function
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the Lon protease is an ATP-dependent serine protease recognized as a key protease up-regulated under oxidative stress and involved in the removal of oxidized proteins, the mitochondrial inner membrane i-AAA protease is a crucial component of the defense against accumulation of carbonylated proteins. Due to the irreversible and unrepairable nature of protein carbonylation, proteolytic elimination of oxidatively damaged polypeptides is the major process of the mitochondrial protein quality control system under oxidative stress as first line of defense
physiological function
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the enzyme can function as a protease or a chaperone and reveal that some of its ATP-dependent biological activities do not require translocation. Enzyme-mediated relief of proteotoxic stress and protein aggregation in vivo can also occur without degradation but is not dependent on robust ATP hydrolysis. Degron binding regulates the activities of the AAA+ Lon protease in addition to targeting proteins for degradation, degron binding regulates Lon ATPase and protease activity in addition to serving a recognition function. Inactivation of cell-division inhibitor SulA in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber
physiological function
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the Lon protease is essential for full virulence in Pseudomonas aeruginosa. The Lon protease is not a traditional regulator
physiological function
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Lon is an ATPase associated with cellular activities protease that controls cell division in response to stress and also degrades misfolded and damaged proteins
physiological function
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AAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. Ability of theLon protease to unfold and degrade model protein substrates beginning at N-terminal, C-terminal, or internal degrons, unfolding with robust and processive unfolding/degradation of some substrates with very stable protein domains, including mDHFR and titin, overview
physiological function
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the ATP-dependent Lon protease is a key component of the quality control system, which ensures the integrity and functionality of cellular proteins
physiological function
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Lon protease is required to suppress the expression of the reb genes. Lon protease is also involved in the regulation of exopolysaccharide production and autoagglutination of bacterial cells
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physiological function
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the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
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physiological function
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purified Lon binds double stranded as well as single stranded DNA in the presence of elevated salt concentrations
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physiological function
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lon disruption mutants show increased UV sensitivity, and produce higher levels of tabtoxin than the wild-type. Strains with lon disruption elicit the host defense system more rapidly and strongly than the wild-type strain, suggesting that the Lon protease is essential for systemic pathogenesis
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physiological function
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ATP-dependent proteases, e.g. represented by Lon, are stress proteins that are induced in bacterial cells in response to unfavourable conditions. The enzyme negatively affects GacA protein stability and expression of the Gac/Rsm signal transduction pathway in Pseudomonas protegens, it is an important negative regulator of the Gac/Rsm signal transduction pathway in the organism. The Gac/Rsm signal transduction pathway controls secondary metabolism and suppression of fungal root pathogens via the expression of regulatory small RNAs, overview
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additional information
the N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones
additional information
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the N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones
additional information
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eukaryotic Lon possesses three domains, an N-terminal domain, an ATPase domain and a proteolytic domain
additional information
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the AAA+ ATPase module and protease domain of Lon are part of a single polypeptide
additional information
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the second alpha-helical domain plays a crucial role in ATP hydrolysis and enzyme binding to the target protein, while the first alpha-helical domain is not important for the manifestation of the catalytic properties of the enzyme, but it affects the functioning of Lon ATPase and peptidase sites and is involved in maintaining enzyme stability, participation of the first alpha-helical domain in the formation of three-dimensional structures of LonA proteases and/or their complexes with DNA
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acid resistance regulator GdE protein + H2O
?
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degradation of GadE protein by Lon rapidly terminates the acid resistance response upon shift back to neutral pH and avoids overexpression of acid resistance genes in stationary phases
-
-
?
acyl-CoA oxidase + H2O
?
-
exhibits little, if any, in vitro acyl-CoA oxidase processing activity
-
-
?
Ald4 + H2O
?
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i.e. potassium-activated aldehyde dehydrogenase, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
alpha-casein-fluorescein isothiocyanate + H2O
?
-
-
-
?
Atp2 + H2O
?
-
i.e. F1F0-ATP synthase subunit beta, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
beta-galactosidase fragment 3-93 + H2O
?
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a 48-residue N-terminal variant and a 33-residue C-terminal variant of beta-galactosidase fragment are degraded very slowly. Lon rapidly degrades a variant containing the 68 N-terminal residues and a variant containing the C-terminal 43 residues of the 3-93 fragment. Residues 49-68, QLRSLNGEWRFAWFPAPEAV play an important role in regocnition by Lon
-
-
?
CNBr-fragments of bovine serum albumin + H2O
?
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less dependent on ATP hydrolysis
-
-
-
CspD + H2O
?
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CspD is a replication inhibitor, which is induced in stationary phase or upon carbon starvation and increases the production of persister cells. CspD is subject to proteolysis by the Lon protease both in vivo and in vitro. Turnover of CspD by Lon is strictly adjusted to the growth rate and growth phase of Escherichia coli, reflecting the necessity to control CspD levels according to the physiological conditions. Truncation or point mutation of CspD does not elevate protein stability
-
-
?
Denatured bovine serum albumin + H2O
?
-
-
-
-
-
Denatured lambda Cro protein + H2O
?
-
poor substrate, inhibits casein hydrolysis
-
-
-
DNA methyltransferase + H2O
?
-
selectively degrades cell-cycle-regulated DNA methyltransferase thereby regulating methylation of chromosomal DNA and cellular differentiation
-
-
?
DNA-binding protein HUbeta + H2O
?
-
Lon binds to both histone-like proteins HUalpha and HUbeta, but selectively degrades only HUbeta in the presence of ATP. Preferred cleavage site is the A20-A21, followed in preference by L36-K37. Degradation of substrate mutants A20D and A20Q is more slowly. Mechanism follows at least three stages: binding of Lon with the HU protein, hydrolysis of ATP by Lon to provide energy to loosen the binding to the HU protein and to allow an induced-fit conformational change, and specific cleavage of only HUbeta
-
-
?
EYLFRHSDNELLHWM + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
F-QLRSLNGEWRFAWFPAPEAV-Q + H2O
F-QLRSLNG + EWRFAWFPAPEAV-Q
-
residues 49–68 of betqa-galactosidase flanked by a fluorophore-quencher pair
-
-
?
FAKYWQAFRQYPRLQ + H2O
?
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
FRETN 89-98Abu + H2O
?
-
peptide-based substrate containing the Y(NO2)-Abz internal fluorescence quenching pair and peptide sequence RGIT-Abu-SGRQK, no substrate for human protease ClpXP
-
-
?
FRQYPRLQGGFVWDW + H2O
?
-
degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
GFP-titinI27-sul20C + H2O
?
-
when degradation initiated at the N-terminus, the full-length substrate disappears about 10fold more rapidly than when degradation initiated at the C-terminus
-
-
?
Gln-Ala-Ala-Phe-p-nitroanilide + H2O
?
-
preferred substrate
-
?
Glu-Ala-Ala-Phe-4-methoxy-2-naphthylamide + H2O
Glu-Ala-Ala-Phe + 4-methoxy-2-naphthylamine
-
-
-
?
glutaryl-AAF-4-methoxy-beta-naphthylamide + H2O
glutaryl-L-Ala-L-Ala-L-Phe + 4-methoxy-2-naphthylamine
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide + H2O
?
-
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
heat shock sigma factor 32 + H2O
?
-
degraded by synergistic action of lon, Clp and HflB
-
-
?
HemA + H2O
?
-
conditional proteolysis mediated by lon and ClpAP
-
-
?
hemoglobin A + H2O
?
can degrade unfolded human hemoglobin A at 70°C either in presence or absence of ATP, at 37°C only in presence of ATP
-
?
homoserine trans-succinylase + H2O
?
-
degraded by synergistic action of lon, ClpYQ, ClpXP and/or ClpAP
-
-
?
HQWRGDFQFNISRYS + H2O
?
-
degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
HSP60 + H2O
?
-
i.e. heat shock protein 60, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
human alphaA-crystallin + H2O
?
-
Lon recognizes conserved determinants in the folded alpha-crystallin domain itself
-
-
?
human alphaB-crystallin + H2O
?
-
Lon recognizes conserved determinants in the folded alpha-crystallin domain itself
-
-
?
HYPNHPLWYTLCDRY + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
IbpA + H2O
?
-
i.e. Escherichia coli small heat shock protein A. Lon degrades purified IbpA substantially more slowly than purified IbpB, which is a consequence of differences in maximal Lon degradation rates and not in substrate affinity. IbpB stimulates Lon degradation of IbpA both in vitro and in vivo. The variable N- and C-terminal tails of the Ibps contain critical determinants that control the maximal rate of Lon degradation
-
-
?
IbpB + H2O
?
-
i.e. Escherichia coli small heat shock protein B. Lon degrades purified IbpA substantially more slowly than purified IbpB, which is a consequence of differences in maximal Lon degradation rates and not in substrate affinity.The variable N- and C-terminal tails of the Ibps contain critical determinants that control the maximal rate of Lon degradation
-
-
?
Ilv5 + H2O
?
-
i.e. ketol acid reductoisomerase, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
LLIRGVNRHEHHPLH + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
Lpd1 + H2O
?
-
i.e. dihydrolipoamide dehydrogenase E3 component of pyruvate dehydrogenase complex, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
LRAGENRLAVMVLRW + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
LTEAKHQQQFFQFRL + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
mitochondrial aconitase + H2O
?
-
essential enzyme, particularly susceptible to oxidative damage, preferentially oxidatively modified and inactivated during ageing
-
?
Mrp20 + H2O
?
-
i.e. mitochondrial subunit of the large ribosomal particle, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
MWRMSGIFRDVSLLH + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
N-glutaryl-alanylalanylphenylalanyl-3-methoxynaphthylamide + H2O
?
-
fluorogenic petide
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-L-leucyl-L-leucine + Val-Tyr-7-amido-4-methylcoumarin + N-succinyl-L-leucine + Leu-Val-Tyr-7-amido-4-methylcoumarin
-
no cleavage of bond between Y and 7-amido-4-methylcoumarin
-
-
?
native aconitase + H2O
?
-
degradation at a lower efficiency than oxidized aconitase
-
-
?
oxidized aconitase + H2O
?
-
oxidatively modified proteins and unfolded peptides are good substrates for proteolysis by lon
-
-
?
Pdb1 + H2O
?
-
i.e. pyruvate dehydrogenase E1component subunit beta, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
Pro-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O
?
-
nonapeptide related to equine angiotensinogen
-
-
-
QLRSLNGEWRFAWFPAPEAV + H2O
QLRSLNG + EWRFAWFPAPEAV
-
variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines and fused with residues 49-68 of beta-galactosidase fragment 3-93
-
-
?
ribulose-1,5-bisphosphate carboxylase/oxygenase + H2O
?
RubiscoTK
-
?
RMVQRDRNHPSVIIW + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RNA
?
-
mitochondrial lon binds preferentially to single-stranded RNA in a sequence-dependent manner
-
-
?
RWDLPLSDMYTPYVF + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWLPAMSERVTRMVQ + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWQFNRQSGFLSQMW + H2O
?
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
S1 peptide + H2O
?
-
decapeptide S1 containing the amino acid residues 89-98 of the bacteriophage lambdaN transcription anti-termination factor, and a fluorescence donor-acceptor pair
-
-
?
Sod2 + H2O
?
-
i.e. mitochondrial superoxide dismutase, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
succinyl-FLF-4-methoxy-beta-naphthylamide + H2O
succinyl-FLF + 4-methoxy-beta-naphthylamine
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
succinyl-Phe-Leu-Phe-4-methoxy-beta-naphthylamide + H2O
?
-
-
?
titin-I27CD + H2O
?
-
variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines
-
-
?
transcription activator SoxS + H2O
?
-
fusion of the C-terminal domain of Rob, which is a transcription activator of the SoxRS/MarA/Rob regulon, to SoxS protects its N-terminus from Lon protease, as Lon's normally rapid degradation of SoxS is blocked in the chimera
-
-
?
Unfolded polypeptides + H2O
short peptides of 5-15 amino acids
-
broad specificity
-
-
Y(3-NO2)-RGIT2-aminobutyric acid-SGRQ-K(anthranilamide) + H2O
Y(3-NO2)-RGIT2-aminobutyrate + SGRQ-K(anthranilamide)
-
-
-
-
?
YLEDQDMWRMSGIFR + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
YRGIT-Abu-SGRQK(Bz) + H2O
?
-
-
-
-
?
YWQAFRQYPRLQGGF + H2O
?
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
Abz-QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A + H2O
?
i.e. F-beta20-Q peptide, a synthetic fluorogenic peptide
-
-
?
Abz-QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A + H2O
?
-
i.e. F-beta20-Q peptide, the substrate is flanked by a fluorophore (Abz) and quencher (nitrotyrosine) pair
-
-
?
alpha-casein + H2O
?
cleavage in an ATP-dependent manner
-
-
?
alpha-casein + H2O
?
cleavage in an ATP-dependent manner
-
-
?
apoTroA + H2O
?
-
a molybdoenzyme; immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation
-
-
?
apoTroA + H2O
?
-
a molybdoenzyme, immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation
-
-
?
ATP + H2O
phosphate + ADP
-
oligomeric organization of lon protease and ATP hydrolysis are necessary prerequisites of realization of the processive degradation of a protein substrate
-
-
?
ATP + H2O
phosphate + ADP
-
high-affinity sites hydrolyze ATP very slowly, but support multiple rounds of peptide hydrolysis, while the low-affinity sites hydrolyze ATP quickly. Affinities of sites differ from one another 10fold. Hydrolysis at both the high- and low-affinity sites are necessary for optimal peptide cleavage and the stabilization of the conformational change associated with nucleotide binding
-
-
?
Bacteriophage lambda protein N + H2O
Hydrolyzed bacteriophage lambda protein N
-
-
-
-
-
Bacteriophage lambda protein N + H2O
Hydrolyzed bacteriophage lambda protein N
-
cleavage sites: Ala16-Gln, Ala-Glu, Ala-Lys, Leu-Asn, Leu-Glu, Ser-Lys, Cys-Ser
-
-
calpain 10 + H2O
?
-
degradation of the mitochondrial matrix protease
-
-
?
calpain 10 + H2O
?
-
degradation of the mitochondrial matrix protease
-
-
?
casein + H2O
?
-
lon contains three distinct domains, an amino-terminal domain having an undefined function, a central ATPase domain crucial for substrate binding and unfolding, and a C-terminal peptidase domain
-
-
?
casein + H2O
hydrolyzed casein
-
alpha-casein
-
-
-
casein + H2O
hydrolyzed casein
-
methylcasein
-
-
-
DNA
?
-
mitochondrial lon binds preferentially to single-stranded DNA in a sequence-dependent manner
-
-
?
FITC casein + H2O
?
-
presence of ATP stimulates reaction 10fold
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
-
cleavage sites: Leu6-Cys(SO3H), Leu17-Val, Ala14-Leu, Val18-Cys(SO3H)
-
-
glutaryl-AAF-4-methoxy-beta-naphthylamide + H2O
glutaryl-L-Ala-L-Ala-L-Phe + 4-methoxy-2-naphthylamine
Q84FG5;
preferred substrate
-
-
?
glutaryl-AAF-4-methoxy-beta-naphthylamide + H2O
glutaryl-L-Ala-L-Ala-L-Phe + 4-methoxy-2-naphthylamine
Q84FG5;
preferred substrate
-
-
?
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
-
hydrolyzed at 3-4% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
-
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
-
hydrolyzed at 3-4% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
-
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
-
-
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
-
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
-
-
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
fluorogenic peptide, 0.3 mM
-
-
-
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
-
hydrolyzed at 6% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
-
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
-
hydrolyzed at 6% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
HilA + H2O
?
-
mediates proteolysis of the central transcription regulatory factor HilA, which controls the correct timing for the expression of virulence genes necessary for host invasion
-
-
?
HilA + H2O
?
-
mediates proteolysis of the central transcription regulatory factor HilA, which controls the correct timing for the expression of virulence genes necessary for host invasion
-
-
?
lambda phage N protein + H2O
?
-
generation of a panel of fluorescent peptides based on the cleavage profile of substrate lambda phage N protein indicates that protease Lon recognizes numerous discontinouos substrate determinants throughout lambda N protein to achieve substrate promiscuity
-
-
?
LasI + H2O
?
Lon is involved in the regulation of quorum-sensing signaling systems in Pseudomonas aeruginosa, the opportunistic human pathogen. The enzyme is part of the acyl-homoserine lactone-mediated QS system LasR/LasI, but LasR/LasI regulation is independent of the RhlR/RhlI system by Lon. QS systems are organized hierarchically: the RhlR/RhlI system is subordinate to LasR/LasI, Lon represses the expression of LasR/LasI by degrading LasI, an HSL synthase, leading to negative regulation of the RhlR/RhlI system, overview
-
-
?
mDHFR protein + H2O
?
-
tittinI27-fusion and sul20C-tagged protein, to direct Lon degradation of a titinI27 domain, either the N or C terminus of this protein is fused to amino acids 3-93 of Escherichia coli beta-galactosidase, an unstructured sequence that contains the b20 degron, degradation
-
-
?
Melittin + H2O
?
-
isolated proteolytic domain exhibits almost no activity toward casein, but hydrolyzes peptide substrates
-
?
Melittin + H2O
?
-
isolated proteolytic domain exhibits almost no activity toward casein, but hydrolyzes peptide substrates
-
?
mitochondrial processing peptidase alpha subunit + H2O
?
-
human lon initiates substrate cleavage at surface exposed sites, lon degrades mitochondrial processing peptidase alpha subunit only when it is folded
-
-
?
mitochondrial processing peptidase alpha subunit + H2O
?
-
is degraded only when it is folded, trypsin-resistant and competent for assembly into an active enzyme
-
-
?
MPPalpha + H2O
?
-
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
-
-
?
MPPalpha + H2O
?
-
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
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage sites
-
-
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage sites
-
-
-
Proteins with highly abnormal conformation + H2O
?
-
one of the heat-shock proteins under control of rpoH operon(htp R)
-
-
-
Proteins with highly abnormal conformation + H2O
?
-
rate-limiting step in breakdown of highly abnormal and some normal proteins
-
-
-
Proteins with highly abnormal conformation + H2O
?
-
catalyzes inital step in the degradation of proteins with abnormal conformation as may result from nonsense or missense mutations, biosynthetic errors or intracellular denaturation
-
-
-
RcsA + H2O
?
-
protein degradation mediates the turnover of damaged proteins
-
?
ribosomal S2 protein + H2O
?
-
degradation of S2 protein occurs in a processive manner. P1 and P3 sites of cleavage products are predominantly occupied by hydrophobic residues
-
-
?
ribosomal S2 protein + H2O
?
-
major lon cleavages sites within the bacterial S2 ribosomal protein located at the interior of the molecule
-
-
?
StAR + H2O
?
-
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
-
-
?
StAR + H2O
?
-
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
?
-
human lon initiates substrate cleavage at surface exposed sites
-
-
?
steroidogenic acute regulatory protein + H2O
?
-
i.e. StAR protein, an endogenous substrate
-
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
best substrate
-
-
-
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
best substrate
-
-
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
hydrolyzed at 137% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
succinyl-FLF-4-methoxy-beta-naphthylamide + H2O
succinyl-FLF + 4-methoxy-beta-naphthylamine
Q84FG5;
-
-
-
?
succinyl-FLF-4-methoxy-beta-naphthylamide + H2O
succinyl-FLF + 4-methoxy-beta-naphthylamine
Q84FG5;
-
-
-
?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
-
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
-
-
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
-
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
fluorogenic peptide, hydrolyzed at 75% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
-
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
-
SulA + H2O
?
-
inactivation of SulA through the enzyme in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber
-
-
?
tmRNA-tagged protein + H2O
?
-
highly purified lon preferentially degrades tmRNA-tagged forms of proteins compared to untagged forms
-
-
?
Y(3-NO2)-RGITCSGRQ-K(anthranilamide) + H2O
Y(3-NO2)-RGITC + SGRQ-K(anthranilamide)
-
-
-
-
?
Y(3-NO2)-RGITCSGRQ-K(anthranilamide) + H2O
Y(3-NO2)-RGITC + SGRQ-K(anthranilamide)
-
-
-
-
?
FRETN 89-98 + H2O
additional information
-
-
peptide-based substrate containing the Y(NO2)-Abz internal fluorescence quenching pair and peptide sequence RGITCSGRQK, also substrate for human protease ClpXP
cleavage of the peptide at Cys-Ser
-
?
additional information
?
-
-
enzyme is required for proper expression, assembly or function of the VirB/D4-mediated T-DNA transfer system
-
-
-
additional information
?
-
-
wild-type shows considerable ATP-dependent activity when assayed at 70°C
-
-
-
additional information
?
-
wild-type shows considerable ATP-dependent activity when assayed at 70°C
-
-
-
additional information
?
-
-
proteolytic domain and a large transmembrane domain insertion within the AAA+ module between the Walker motifs A and B
-
-
-
additional information
?
-
-
substrate specificity of isoforms LonA, LonB and of protease Clp can be determined, in part, by the spatial and temporal organization of the proteases in vivo
-
-
-
additional information
?
-
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
-
-
-
additional information
?
-
-
the ATPase and the proteolytic domains function independently. Introduction of a mutation into the proteolytic domain does not affect the ability of Lon-1 to hydrolyze ATP. Lon-1 does not degrade Borrelia-SsrA tagged reporter protein in vitro
-
-
-
additional information
?
-
the ATPase and the proteolytic domains function independently. Introduction of a mutation into the proteolytic domain does not affect the ability of Lon-1 to hydrolyze ATP. Lon-1 does not degrade Borrelia-SsrA tagged reporter protein in vitro
-
-
-
additional information
?
-
the ATPase and the proteolytic domains function independently. Introduction of a mutation into the proteolytic domain does not affect the ability of Lon-1 to hydrolyze ATP. Lon-1 does not degrade Borrelia-SsrA tagged reporter protein in vitro
-
-
-
additional information
?
-
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
-
-
-
additional information
?
-
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
-
-
-
additional information
?
-
-
No substrates are native bovine serum albumin, hemoglobin
-
-
-
additional information
?
-
-
No substrates are native bovine serum albumin, hemoglobin
-
-
-
additional information
?
-
-
No substrates are glutaryl-Phe-7-amino-4-methylcoumarin, Ala-Ala-Phe-methoxynaphthylamide, Gly-Phe-methoxynaphthylamide, Asp-methoxynaphthylamide, Leu-methoxynaphthylamide, Arg-methoxynaphthylamide, Ala-methoxynaphthylamide, Tyr-methoxynaphthylamide, Lys-methoxynaphthylamide, methoxyglutaryl-Ala-Ala-Phe-methoxynaphthylamide, methoxysuccinyl-Ala-Ala-Phe-methoxynaphthylamide, benzyloxycarbonyl-Ala-Pro-methoxynaphthylamide, benzoyl-Arg-Gly-Phe-Phe-Leu-methoxynaphthylamide, benzoyl-Arg-Gly-Leu-methoxynaphthylamide, Leu-Gly-Gly-methoxynaphthylamide, Ser-Tyr-methoxynaphthylamide
-
-
-
additional information
?
-
-
No substrates are lambda-repressors cI and Cro, lambda replication protein O, E. coli galactose repressor, even after heat denaturation
-
-
-
additional information
?
-
-
the active site prefers hydrophobic substrate sequences
-
-
-
additional information
?
-
-
mutant enzyme in which active site Ser-679 is replaced by Ala lacks peptidase but retains ATPase activity
-
-
-
additional information
?
-
-
no phosphorylation of enzyme or substrate during ATP hydrolysis
-
-
-
additional information
?
-
-
with a proteolytic and an ATP-binding site per monomer
-
-
-
additional information
?
-
-
No substrates are benzyloxycarbonyl-Ala-Arg-Arg-methoxynaphthylamide, native or denatured ribonuclease, native or denatured lysozyme, native immunoglobulin G
-
-
-
additional information
?
-
-
can bind to a TG-rich DNA promoter element in a sequence-specific manner
-
?
additional information
?
-
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isolated proteolytic domain exhibits the peptidase activity
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?
additional information
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essential for growth of yeast on nonfermentable carbon sources
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additional information
?
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rapid proteolysis plays a major role in post-translational cellular control by the targeted degradation of short-lived regulatory proteins
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?
additional information
?
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recognition and selective degradation of abnormal and unstable proteins
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?
additional information
?
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regulation of several important cellular functions, including radiation resistance, cell division, filamentation, capsular polysaccharide production, lysogeny of certain bacteriophages, and proteolytic degradation of certain regulatory and abnormal proteins
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?
additional information
?
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enzyme and protease Clp participate in the physiological disintegration of cytoplasmic inclusion bodies, their absence minimizing the protein removal up to 40%. Clp takes the major and enzyme a minor role in processing of aggregation-prone proteins and also of polypeptides physiologically released from inclusion bodies
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additional information
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the polyphosphate-lon complex does not degrade intact native ribosomes
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additional information
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proteolytic domain and a a large N-terminal domain, active site has a Ser-Lys catalytic dyad. Proteolytic domain exhibits no detectable activity against protein substrates degraded by full-length lon, but retains a significant fraction of peptidase activity
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additional information
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protease Lon recognizes specific sequences rich in aromatic residues that are accessible in unfolded polypeptides but hidden in most native structures. Denatured polypeptides lacking such sequences are poor substrates. Lon also unfolds and degrades stably folded proteins with accessible recognition tags. Lon can recognize multiple signals in unfolded polypeptides synergistically, resulting in nanomolar binding and a mechanism for discriminating irreversibly damaged proteins from transiently unfolded elements of structure
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additional information
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enzyme recognizes degrons, i.e. degradation tags. Degron tags are also regulatory elements that determine protease activity levels. Different tags fused to the same protein change degradation speeds and energetic efficiencies by 10fold or more. Degron binding to multiple sites in the Lon hexamer differentially stabilizes specific enzyme conformations, including one with high protease and low ATPase activity, and results in positively cooperative degradation
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additional information
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Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible. The half-site ATPase reactivity of Lon can be used to account for the kinetic mechanism of the ATP-dependent peptidase activity of the enzyme
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additional information
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the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
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additional information
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homooligomeric ATP-dependent LonA proteases are bifunctional enzymes
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additional information
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repeated cycles of ATP binding and hydrolysis power conformational changes that pull the tag through the pore and eventually tug the native portion of the substrate against the AAA+ ring, creating an unfolding force. Depending on the native substrate and enzyme, successful unfolding can require anywhere from a few to many hundreds of cycles of ATP hydrolysis
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additional information
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compared with hexamers, enzyme dodecamers are much less active in degrading large substrates but equally active in degrading small substrates, whcih represents a a unique gating mechanism that allows the repertoire of enzyme substrates to be tuned by its assembly state
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additional information
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native enzyme hydrolyzes ATP in the absence of a protein substrate
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additional information
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substrate specifiicty, overview. GFP-fusion proteins resist Lon degradation from the N-terminus. Partially degraded substrate fragments accumulate as proteolytic products, which is often observed during degradation in vitro of multi-domain substrates containing very stable interior domains
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additional information
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isolated proteolytic domain exhibits the peptidase activity
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?
additional information
?
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can bind to a TG-rich DNA promoter element in a sequence-specific manner
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?
additional information
?
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regulation of several important cellular functions, including radiation resistance, cell division, filamentation, capsular polysaccharide production, lysogeny of certain bacteriophages, and proteolytic degradation of certain regulatory and abnormal proteins
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?
additional information
?
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proteomes of wild-type and a lon-abi conditional mutant are compared by quantitative high-throughput proteomics in order to understand the global impact of the LonB protease on archaeal physiology and to discover its potential protein substrates. Proteins enriched in the lon mutant (soluble and membrane associated polypeptides) represent potential natural substrates of the membrane protease LonB
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additional information
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proteomes of wild-type and a lon-abi conditional mutant are compared by quantitative high-throughput proteomics in order to understand the global impact of the LonB protease on archaeal physiology and to discover its potential protein substrates. Proteins enriched in the lon mutant (soluble and membrane associated polypeptides) represent potential natural substrates of the membrane protease LonB
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additional information
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participates directly in the metabolism of mitochodrial DNA
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?
additional information
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ATP stimulated protease may be an essential defence against the stress of life in an oxygen environment
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?
additional information
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enzyme participates directly in the metabolism of mitochondrial DNA
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additional information
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lon interacts with the mitochondrial genome in cultured cells. Associates with sites distributed primarily within one-half of the genome and preferentially with the control region for mitochondrial DNA replication and transcription, which has a G-rich consensus sequence
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additional information
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does not process PTS2 protein-containing 3-ketoacyl-coenzyme A thiolase
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additional information
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the enzyme and sirtuin 3 interact, but sirtuin 3 is not a substrate for Lon activity
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additional information
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lacking the ATPase domain
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?
additional information
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the enzyme selectively degrades unfolded protein substrates in an ATP-independent manner, structural basis of substrate recognition, overview
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additional information
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mediates the degradation of misfolded, unassembled or oxidatively damaged polypeptides, not only degrades protein substrates but also binds DNA, specifically binds to single stranded but not to double-stranded DNA oligonucleotides
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?
additional information
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succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin-7-amide is not cleaved
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?
additional information
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lacks 90, 225, or 277 N-terminal residues, practically no proteolytic activity while exhibiting reduced protein binding activity
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additional information
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Lon can efficiently and selectively degrade tmRNA-tagged proteins. The larger, 27 amino acids long, tmRNA tag contains multiple discrete signalling motifs for efficient recognition and rapid degradation by Lon. Lon-mediated degradation process absolutely depends on the presence of ATP, and tmRNA-tagged reporter protein degradation is dependent on the presence of full-length tmRNA tag
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additional information
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protease Lon represses the expression of LasR/LasI by degrading HSL synthase LasI, leading to negative regulation of the RhlR/RhlI system. RhlI/RhlR is also regulated by Lon independently of LasI/LasR
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additional information
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protease Lon represses the expression of LasR/LasI by degrading HSL synthase LasI, leading to negative regulation of the RhlR/RhlI system. RhlI/RhlR is also regulated by Lon independently of LasI/LasR
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additional information
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is a negative regulator of acyl homoserine lactone production
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additional information
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is a negative regulator of acyl homoserine lactone production
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additional information
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is a negative regulator of acyl homoserine lactone production
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additional information
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protease and ATPase activity, bovine serum albumin is no substrate
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?
additional information
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involved in mitochondrial protein turnover
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additional information
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required for expression of intron-containing genes in mitochondria, required for selective proteolysis in the matrix, maintenance of mitochondrial DNA, and respiration-dependent growth
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?
additional information
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required for mitochondrial function
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?
additional information
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required for selective proteolysis in the matrix, maintenance of mitochondrial DNA, and respiration-dependent growth
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?
additional information
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required for selective proteolysis in the matrix, maintenance of mitochondrial DNA, and respiration-dependent growth, protein degradation in mitochondrial homeostasis
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?
additional information
?
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enzyme recognizes specific surface determinants or folds, initiates proteolysis at solvent-accessible sites, and generates unfolded polypeptides that are then processively degraded
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additional information
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construct containing residues 793-1133 of yeast lon, which comprises the proteolytic domain along with most of the alpha-domain, exhibits low but significant proteolytic activity in vivo
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additional information
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endogenous substrates, which are misfolded or unassembled subunits of electron transport chain complexes, ribosomal proteins and metabolic enzymes
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additional information
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yeast lon has a relatively poor ability to unravel proteins and is only able to degrade proteins that have unstable tertiary structure
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additional information
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belonging to AAA+ superfamily
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?
additional information
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proteases ClpXP and Lon contribute to the environmental regulation of type III secretion system T3SS through regulated proteolysis of small histone-like protein YmoA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acid resistance regulator GdE protein + H2O
?
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degradation of GadE protein by Lon rapidly terminates the acid resistance response upon shift back to neutral pH and avoids overexpression of acid resistance genes in stationary phases
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?
apoTroA + H2O
?
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a molybdoenzyme; immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation
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?
LasI + H2O
?
Q9I2T9
Lon is involved in the regulation of quorum-sensing signaling systems in Pseudomonas aeruginosa, the opportunistic human pathogen. The enzyme is part of the acyl-homoserine lactone-mediated QS system LasR/LasI, but LasR/LasI regulation is independent of the RhlR/RhlI system by Lon. QS systems are organized hierarchically: the RhlR/RhlI system is subordinate to LasR/LasI, Lon represses the expression of LasR/LasI by degrading LasI, an HSL synthase, leading to negative regulation of the RhlR/RhlI system, overview
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?
mitochondrial aconitase + H2O
?
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essential enzyme, particularly susceptible to oxidative damage, preferentially oxidatively modified and inactivated during ageing
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?
calpain 10 + H2O
?
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degradation of the mitochondrial matrix protease
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?
calpain 10 + H2O
?
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degradation of the mitochondrial matrix protease
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?
Proteins with highly abnormal conformation + H2O
?
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one of the heat-shock proteins under control of rpoH operon(htp R)
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Proteins with highly abnormal conformation + H2O
?
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rate-limiting step in breakdown of highly abnormal and some normal proteins
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Proteins with highly abnormal conformation + H2O
?
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catalyzes inital step in the degradation of proteins with abnormal conformation as may result from nonsense or missense mutations, biosynthetic errors or intracellular denaturation
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RcsA + H2O
?
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protein degradation mediates the turnover of damaged proteins
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?
SulA + H2O
?
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inactivation of SulA through the enzyme in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber
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-
?
additional information
?
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enzyme is required for proper expression, assembly or function of the VirB/D4-mediated T-DNA transfer system
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additional information
?
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substrate specificity of isoforms LonA, LonB and of protease Clp can be determined, in part, by the spatial and temporal organization of the proteases in vivo
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additional information
?
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essential for growth of yeast on nonfermentable carbon sources
-
-
-
additional information
?
-
-
rapid proteolysis plays a major role in post-translational cellular control by the targeted degradation of short-lived regulatory proteins
-
?
additional information
?
-
-
recognition and selective degradation of abnormal and unstable proteins
-
?
additional information
?
-
-
regulation of several important cellular functions, including radiation resistance, cell division, filamentation, capsular polysaccharide production, lysogeny of certain bacteriophages, and proteolytic degradation of certain regulatory and abnormal proteins
-
?