3.4.21.53: Endopeptidase La
This is an abbreviated version!
For detailed information about Endopeptidase La, go to the full flat file.
Reaction
hydrolysis of proteins in presence of ATP
=
Synonyms
AAA+ Lon protease, AAA+ protease, AAAP, AF0364, AfLon, archaeal Lon protease, ATP-dependent lon protease, ATP-dependent Lon proteinase, ATP-dependent PIM1 protease, ATP-dependent protease La, ATP-dependent protease lon, ATP-dependent protease LonA, ATP-dependent serine proteinase, ATP-independent Lon-like protease, bacterial protease lon, BPP1347, ClpXP, EcLon, Ec-Lon, Ec-Lon protease, EcLon, EcLon protease, ELon, Escherichia coli proteinase La, Escherichia coli serine proteinase La, Gene lon protease, Gene lon proteins, hLon, human ATP-dependent protease, human lon protease, HVO_0783, i-AAA Protease, la, La protease, lon, lon (la) protease, lon (Pim1p) protease, Lon AAA+ protease, lon ATP-dependent protease, lon protease, LON protease 1, Lon protein, Lon proteinase, lon-like protease, Lon-like-Ms, lon1, lon2, lon3, lon4, lonA, lonB, lonB protease, LonC, LonC protease, lonD, LONP1, lonR9, LONRF1, lonS, lonTK, lonV, mitochondrial ATP-dependent protease, mitochondrial ATP-dependent protease La, mitochondrial Lon protease, MLon, Ms-Lon, Msm 1754, Msm_1754, MtaLonA, MtaLonC, Nmag_2822, NmLon, non-canonical RNA viral Lon proteinase, peroxisomal Lon protease, PIM1, PIM1 protease, PIM1 proteinase, Pim1p, PLon, protease, Protease La, protease lon, Proteinase La, Proteinase, Escherichia coli serine, La, Proteinase, La, Proteins, gene lon, Proteins, specific or class, gene lon, ScLon, serine protease, Serine protease La, Ta1081, Thela2p4_005149, Thela2p4_006664, TK1264, TonLonB, TON_0529, yeast mitochondrial lon, yeast protease
ECTree
Application
Application on EC 3.4.21.53 - Endopeptidase La
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
biotechnology
-
protein synthesis in Escherichia coli, 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
diagnostics
-
high levels of LONP1 are a poor prognosis marker in human colorectal cancer and melanoma
agriculture
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
agriculture
-
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
-
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
medicine
-
lon downregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins
medicine
-
lon downregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins. Oppositely modulates infection stages (epithelial invasion and survival within murine macrophages)
medicine
-
lon downregulation may contribute to the aging process
medicine
-
lon downregulation may contribute to the aging process
medicine
-
lon is a target in the development of antibiotics
medicine
-
lon is involved in eliminating misfolded proteins, may contribute to the virulence of Campylobacter jejuni
medicine
-
lon mediates proteolysis for the expression of virulence genes that promote mammalian cell infection
medicine
-
lon mediates proteolysis for the expression of virulence genes that promote mammalian cell infection
medicine
-
lon upregulates virulence, is involved in transcriptional regulation of type three secretion systems to translocate virulence proteins
medicine
-
potential therapeutic antimicrobial target to combat fluoroquinolone resistance
medicine
-
subinhibitory concentrations of antibiotics induce a set of genes, e.g. lon protease, that are likely to affect the interaction of Pseudomonas aeruginosa with host cells. lon protease is essential for biofilm formation and motility in Pseudomonas aeruginosa
medicine
-
in muscle creatine kinase mouse heart model for Friedreich ataxia, a rare hereditary neurodegenerative disease characterized by progressive ataxia and cardiomyopathy, there is a clear progressive increase in protein levels of mitochondrial ATP-dependent proteases, Lon and ClpP, in the hearts of muscle creatine kinase mutants. Lon and ClpP upregulation, which is triggered at a mid-stage of the disease through separate pathways, is accompanied by an increase in proteolytic activity. There is a simultaneous and significant progressive loss of mitochondrial Fe-S proteins with no substantial change in their mRNA level
medicine
-
lon single and cpxR and lon double mutants 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
medicine
-
lon is involved in eliminating misfolded proteins, may contribute to the virulence of Campylobacter jejuni
-
additional information
-
functions in protein quality control
additional information
-
induction of lon contributes to the adaptive resistance of the organism towards antibiotic treatment
additional information
-
lon causes proteolysis of normal proteins in cells and is lethal to host cells. lon-polyphosphate complex is the missing link between protein degradation and the phenomen of stringent response. The complex between lon and polyphosphate is formed during the stringent response, whereon degrades at lest free ribosomal proteins, providing amino acids for synthesizing enzymes required for adaption to a nutrient-poor environment
additional information
-
lon is involved in the control of swarmer cell differentiation
additional information
-
lon is required for cell cycle-dependent regulation of methylation, correct completion of cell division and normal progression of the cell cycle
additional information
-
lon may be an important defense mechanism to protect mitochondria of steroidogenic cells against oxidative damage induced by steroid hydroxylation and to maintain the level of postfunctional steroidogenic acute regulatory protein compatible with mitochondrial homeostasis
additional information
-
lon plays a role in protein quality control by destroying unfolded proteins, it participates in regulatory circuits by controlling amount and availability of specific substrates
additional information
-
lon protease functions in trans translation
additional information
-
lonA plays a major role in initiating sporulation in response to environmental conditions, lonB is forespore-specific and may have a limited role in the regulation of sporulation
additional information
-
lonV gene is essential for viability, lonD gene is essential for spore and fruiting body formation
additional information
-
plays vital roles in maintaining cellular functions by selectively eliminating misfolded, damaged and certain short-lived regulatory proteins. lon is essential for cellular homeostasis, mediating protein quality control and metabolic regulation
additional information
-
roles for lon in linking protein and mitochondrial DNA quality control
additional information
-
stress response network between the endoplasmic reticulum, nucleus and mitochondrion up-regulates the expression, thereby providing a cytoprotective function during endoplasmic reticulum stress and hypoxia
additional information
-
stress response network between the endoplasmic reticulum, nucleus and mitochondrion up-regulates the expression, thereby providing a cytoprotective function during endoplasmic reticulum stress and hypoxia