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
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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
Cofactor
Cofactor on EC 3.4.21.53 - Endopeptidase La
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ADP
results in 72% activity with substrate alpha-casein, and 64% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+
GTP
results in 85% activity with substrate alpha-casein, and 90% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+
AMPPNP
5'-adenylyl imidodiphosphate, results in 80% activity with substrate alpha-casein, and 92% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+
AMPPNP
adenylylimidodiphosphate, is not as effective as ATP, slight activation
ATP
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ATP
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at physiological concentrations
ATP
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effect of enzyme purification or storage on stimulation by ATP
ATP
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enzyme tetramer has two high and two low affinity binding sites for ATP
ATP
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proteolytically inactive mutant enzyme with completely unaffected ATPase activity
ATP
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two ATP molecules are hydrolyzed for each peptide bond cleaved in proteins
ATP
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only phosphate is released after ATP hydrolysis
ATP
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ADP remains on the enzyme
ATP
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binds to enzyme as allosteric activator allowing peptide bond hydrolysis with subsequent ATP hydrolysis
ATP
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ATP-binding is reversible
ATP
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activation only in the presence of Mg2+
ATP
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activation only in the presence of Mg2+
ATP
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MgATP2- rather than ATP4-
ATP
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ATP- or ATP-analog-binding in the presence of EDTA
ATP
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splitting of high-energy bond of ATP is required for protein breakdown
ATP
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ATP-dependent protease
ATP
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ATP-dependent protease
29339, 29340, 29342, 29343, 29344, 29345, 29346, 29347, 29348, 29349, 29350, 29351, 29352, 29353, 29354, 29356, 29357, 29358, 29359, 29360, 29361
ATP
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ATP-dependent protease
ATP
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ATP-dependent protease
ATP
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ATP-dependent protease
ATP
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ATP-dependent protease
ATP
ATP-dependent protease
ATP
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MnATP2- or CaATP2- rather than ATP4-
ATP
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ATP hydrolysis is not stoichiometrically linked with proteolysis
ATP
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ATP hydrolysis is essential for hydrolysis of proteins
ATP
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ATP hydrolysis is essential for hydrolysis of proteins
ATP
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enzyme tetramer has high and low affinity binding sites for ATP
ATP
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rapid depletion of ATP prevents proteolysis
ATP
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enzyme binds 4 mol ATP per tetramer
ATP
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enzyme binds 4 mol ATP per tetramer at ATP concentrations above 0.01 mM
ATP
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enzyme binds 2 mol ATP/tetramer in the absence of divalent cations or at 0.01 mM ATP in the presence of Mn2+ or Mg2+
ATP
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diphosphate, adenyl-5'-yl methylene diphosphate, GTP, UTP and CTP at 1 mM have no effect on the binding of ATP to the enzyme
ATP
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ATP hydrolysis is not essential for hydrolysis of peptides
ATP
-
physiological activator
ATP
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binding of ATP induces a conformational change that facilitates the coupling of nucleotide hydrolysis with peptide substrate delivery to the peptidase active site
ATP
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ATPase domain that includes AAA+ modules
ATP
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ATPase domain that includes AAA+ modules
ATP
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best activator of the peptidase activity
ATP
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in the absence of ATP, no peptide cleavage is observed
ATP
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in the absence of ATP, no peptide cleavage is observed
ATP
-
low-affinity and high-affinity ATP sites
ATP
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optimal peptide cleavage by lon requires hydrolysis of ATP to fully activate the proteolytic site
ATP
-
a ofmitochondrial ATP-dependent protease
ATP
-
ADP bound to the ATPase region stabilizes the enzyme
ATP
ATP-dependent protease, the enzyme contains an AAA-like domain that lacks the conserved ATPase motifs. The LonC AAA-like domain is inserted with a large domain predicted to be largely alpha-helical, the unique Lon-insertion domain is disordered in the full-length crystal structure of Meiothermus taiwanensis LonC
ATP
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protease La is an ATP-dependent protease, it requires ATP hydrolysis to digest larger, intact proteins, but can cleave small, fluorogenic peptides such as Glu-Ala-Ala-Phe-MNA by only binding, but not hydrolyzing, ATP
ATP
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activates, the ATP-binding site is situated at the interface between the alpha/beta-subdomain and the alpha-subdomain. Motifs for ATP hydrolysis and nucleotide sensing are well conserved at the interface. Structure, detailed overview
ATP
ClpXP is a ATP-dependent protease. ClpXP displays a basal rate of ATP hydrolysis even when not engaged in protein degradation and in the presence of ssrA-tagged substrate PR65/A, although not with UCH-L1-ssrA, the ATPase rate is stimulated
ATP
conformational changes are induced by ATP binding and hydrolysis
ATP
-
dependent on, stimulation of ATPase activity by substrates. The ATPase cycle of the basic residue(s) adjoining the substrate-binding groove of LonA is involved in substrate degradation
ATP
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required, protein degradation by Lon is dependent on energy obtained from ATP hydrolysis, modelng of the structure of hexameric ATPase domain of EcLon protease using the comparative modeling approach, overview
CTP
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activation
CTP
-
hydrolysis at 82% the rate of ATP, supports proteolysis with 31% the efficiency of ATP
CTP
-
less efficient than ATP
CTP
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less efficient than ATP
CTP
results in 122% activity with substrate alpha-casein, and 131% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+
dATP
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activation
dATP
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supports proteolysis with 75% the efficiency of ATP
dATP
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supports proteolysis with 92% the efficiency of ATP
UTP
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activation
UTP
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less efficient than ATP
UTP
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less efficient than ATP
UTP
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hydrolysis at 77% the rate of ATP, supports proteolysis with 22% the efficiency of ATP
UTP
results in 55% activity with substrate alpha-casein, and 64% with peptide substrate glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide compared to ATP in presence of Mg2+
additional information
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adenylyl 5-imidodiphosphate, can replace ATP, shows a reduced peptidase activity
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additional information
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maintenance of the holoenzyme does not require the addition of ATP. ATP binding induces conformational changes in the holoenzyme
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additional information
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oligomerization is independent of ATP
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additional information
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oligomerization is independent of ATP
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additional information
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an ATP-independent Lon-like protease
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additional information
Mg2+-activated LonA degrades unfolded protein or peptides without ATP
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additional information
replacement of ATP by its non-hydrolyzable analogue (AMP-PNP) leads to a marked decrease in the substrate transformation rate and a change of the mechanism of casein hydrolysis for nonprocessive
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