3.4.21.53: Endopeptidase La
This is an abbreviated version!
For detailed information about Endopeptidase La, go to the full flat file.
Word Map on EC 3.4.21.53
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3.4.21.53
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antiretroviral
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transcriptase
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cathepsins
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plasminogen
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coagulation
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hiv-infected
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thrombin
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elastase
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virological
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nucleoside
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neutrophil
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viruses
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endothelial
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pancreatic
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chymotrypsin
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lysosomal
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cd4
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collagen
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leukocyte
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plasmin
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caspase
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calpains
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proteasome
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platelet
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metalloproteinase
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amyloid
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anticoagulant
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clot
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kallikreins
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amylase
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heparin
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fibrinogen
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upa
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venom
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urokinase
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fibrin
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sars-cov-2
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mast
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covid-19
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coronavirus
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zymography
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thrombotic
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antithrombin
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papain
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urokinase-type
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pai-1
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fibrinolytic
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granzyme
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tissue-type
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tryptase
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medicine
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biotechnology
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agriculture
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diagnostics
- 3.4.21.53
-
antiretroviral
- transcriptase
- cathepsins
- plasminogen
- coagulation
-
hiv-infected
- thrombin
- elastase
-
virological
- nucleoside
- neutrophil
- viruses
- endothelial
- pancreatic
- chymotrypsin
- lysosomal
- cd4
- collagen
- leukocyte
- plasmin
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caspase
- calpains
- proteasome
- platelet
- metalloproteinase
-
amyloid
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anticoagulant
- clot
- kallikreins
- amylase
- heparin
- fibrinogen
- upa
- venom
- urokinase
- fibrin
- sars-cov-2
-
mast
- covid-19
- coronavirus
-
zymography
-
thrombotic
- antithrombin
- papain
-
urokinase-type
- pai-1
-
fibrinolytic
-
granzyme
-
tissue-type
- tryptase
- medicine
- biotechnology
- agriculture
- diagnostics
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
3.4.21.53 Endopeptidase LaAdvanced search results
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results (Activating Compound
Activating Compound on EC 3.4.21.53 - Endopeptidase La
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Adenosine 2',3'-dialdehyde triphosphate
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activation, hydrolysis at 23% the rate of ATP, supports proteolysis with 30% the efficiency of ATP
Adenosine 5'-(alpha-thio)triphosphate
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activation, Rp-diastereoisomer stimulates peptide hydrolysis much more effectively than Sp-diastereoisomer
adenyl-5'-yl methylene monophosphonate
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i.e. AMP-CPP, activation, competes for the two ATP-high affinity sites
Bovine glucagon
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activation, glutaryl-Ala-Ala-Phe methoxynaphthylamide hydrolysis, with or without ATP, not casein hydrolysis
degron
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degron binding to this site is not required for proteolysis of sul20-tagged substrates in vitro but enhances degradation by allosterically activating protease activity. Sul20 degron from the cell-division inhibitor SulA binds to the N domain of the enzyme, determination of the recognition site, overview. Allosteric role for the sul20-binding site in the N domain
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Denatured calf thymus or E. coli DNA
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stimulation of glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis
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spermidine
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activation, at physiological concentration, ATP hydrolysis and protease activity
adenosine 5'-(3-thiotriphosphate)
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i.e. adenosine 5'-O-(thiotriphosphate) or ATP-gamma-S, activation
adenosine 5'-(3-thiotriphosphate)
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equally effective as ATP with casein as substrate
adenosine 5'-(3-thiotriphosphate)
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hydrolysis, peptide not protein hydrolysis
adenosine 5'-(3-thiotriphosphate)
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activates, hydrolysis of casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide
Adenyl-5'-yl imidodiphosphate
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casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis
Adenyl-5'-yl imidodiphosphate
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i.e. AMP-PNP, activation
Adenyl-5'-yl imidodiphosphate
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competes for one of the ATP-high-affinity binding-sites
Adenyl-5'-yl imidodiphosphate
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no activation of bovine serum albumin hydrolysis
adenyl-5'-yl methylene diphosphonate
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i.e. AMP-PCP, activation
adenyl-5'-yl methylene diphosphonate
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casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis
ATP
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human mitochondrial lon degrades mouse StAR in the presence of ATP, but not in its absence
ATP
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enzyme does not exhibit any proteolytic activity in the presence of ADP or AMPPCP, a nonhydrolyzable ATP analog
ATP
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hydrolysis of FITC casein is 10fold increase in presence of ATP
ATP
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enzyme needs ATP for its activity and stability. Properties compared with ATP-dependent proteases from different sources
casein
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activation, glutaryl-Ala-Ala-Phe-methoxynaphthylamide or insulin B-chain hydrolysis, in the absence of ATP and synergistic with ATP
Denatured bovine serum albumin
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glutaryl-Ala-Ala-Phe methoxynaphthylamide hydrolysis, with or without ATP
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DNA
Escherichia coli Lon binds both single stranded DNA (ssDNA) and RNA (ssRNA), and double stranded DNA (dsDNA) in a non-specific manner, and this interaction enhances Lon ATPase and proteolytic activities
GTP
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hydrolysis at 113% the rate of ATP, supports proteolysis with 14% the efficiency of ATP
Polyphosphate
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changes substrate preference of enzyme and its oligomeric structure
Polyphosphate
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upon binding to a site in the ATPase domain, stimulation of degradation of ribosomal protein and inhibition of DNA-enzyme complex formation
Polyphosphate
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forms a complex with lon, which enables lon to degrade free ribosomal proteins. Polyphosphate with a shorter chain length is less potent in stimulating. Polyphosphate-binding site is within the ATPase domain fo lon between amino acids 320 and 437
Polyphosphate
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its binding within the ATPase domain of lon promotes the specific association and degradation of free ribosomal proteins
Polyphosphate
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stimulates lon proteolytic activity, affects substrate preference and oligomeric state of the enzyme
Polyphosphate
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stimulates lon-mediated proteolysis of free ribosomal proteins and thereby down-regulates translation
Protein substrates
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stimulation of ATP hydrolysis triggers activation of the proteolytic function
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Protein substrates
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rise in ATPase activity proportional to peptide bonds cleaved
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Protein substrates
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protein substrates, e.g. denatured bovine serum albumin induce ADP-release and promote ATP-ADP-exchange
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Protein substrates
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protein substrates enhance additively the stimulating effect of ATP on peptide hydrolysis and even in the absence of ATP they enhance the ability to degrade fluorogenic tripeptides
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additional information
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lonA gene is induced by heat and salt, lonB is not stress-induced
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additional information
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enzyme hydroylzes proteins and ATP in a coupled process
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additional information
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nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins
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additional information
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enzyme hydroylzes proteins and ATP in a coupled process
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additional information
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enzyme hydroylzes proteins and ATP in a coupled process
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additional information
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peptide substrates, e.g. glutaryl-Ala-Phe-Phe methoxynaphthylamide or succinyl-Phe-Leu-Phe methoxynaphthylamide do not support ATP hydrolysis
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additional information
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no activation by benzoyl-Arg-Gly-Phe-Phe-Leu methoxynaphthylamide (glutaryl-Ala-Ala-Phe methoxynaphthylamide as substrate), poly(A)
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additional information
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no activation by nonhydrolyzable proteins, e.g. native or denatured ribonuclease or lysozyme
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additional information
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nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins
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additional information
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protein degradation requires nucleoside triphosphate hydrolysis, cleavage of small peptides only requires binding of nucleotides to the enzyme
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additional information
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ATP cannot be replaced by adenosine 5'-(beta-thiotriphosphate)
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additional information
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degradation of proteins stimulates ATPase activity of lon
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additional information
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the enzyme activity of Lon can be stimulated by the presence of unfolded proteins (e.g. apomyoglobin, glucagon, and alpha-casein) as well as inorganic polyphosphate accumulated during amino acid starvation
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additional information
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both ATPase and peptidase activities can be stimulated by the binding of a larger protein substrate, such as beta-casein
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additional information
binding of protein substrates by Lon stimulates its ATPase and peptidase activities and that this activation is likely to be allosteric
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additional information
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binding of protein substrates by Lon stimulates its ATPase and peptidase activities and that this activation is likely to be allosteric
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additional information
substrate binding stimulates the enzyme's ATPase activity, 1.37 to 2.39fold, overview
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additional information
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substrate binding stimulates the enzyme's ATPase activity, 1.37 to 2.39fold, overview
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additional information
magnesium-dependent activation and hexamerization of the Lon AAA+ protease
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additional information
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stimulation of ATPase activity by substrates
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additional information
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stimulated by unfolded protein and supported by nonhydrolyzed nucleotide analogs
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additional information
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stimulated by unfolded protein and supported by nonhydrolyzed nucleotide analogs>
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additional information
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oligomerization is stimulated by unfolded protein
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additional information
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enzyme hydroylzes proteins and ATP in a coupled process
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additional information
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nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins
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additional information
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expression of lon increases over time when bacteria are grown in subinhibitory ciprofloxacin concentrations. Subinhibitory antibiotic environments contribute to the development of resistance
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additional information
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enzyme hydroylzes proteins and ATP in a coupled process
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additional information
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nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins
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additional information
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ATP cannot be replaced by nucleoside diphosphates, nucleoside monophosphates, 5'-adenylyl-betagamma-methylene diphosphate, NADP+, NAD+
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additional information
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in heart mitochondria, lon expression increases with age, its ATP-stimulated activity remains the same in young and old cells
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additional information
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enzyme hydroylzes proteins and ATP in a coupled process
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additional information
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nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins
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additional information
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no activation by mRNA, tRNA, poly(rA), (dT)10
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additional information
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activity of yeast lon alpha-proteolytic fragment enhanced when it is coexpressed with a construct containing the N- and A-domains (residues 1-917)
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additional information
substrate binding stimulates the enzyme's ATPase activity
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additional information
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substrate binding stimulates the enzyme's ATPase activity
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