Information on EC 3.4.21.53 - Endopeptidase La

Word Map on EC 3.4.21.53
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.53
-
RECOMMENDED NAME
GeneOntology No.
Endopeptidase La
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins in presence of ATP
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
linked with ATP hydrolysis
-
CAS REGISTRY NUMBER
COMMENTARY hide
79818-35-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene lon
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NCTC11168
-
-
Manually annotated by BRENDA team
strain NCTC11168
-
-
Manually annotated by BRENDA team
strain K12 MG1655
-
-
Manually annotated by BRENDA team
strain MH-1
-
-
Manually annotated by BRENDA team
strain RGC123
-
-
Manually annotated by BRENDA team
strain Y1089
-
-
Manually annotated by BRENDA team
wild-type and mutant strain HVLON3
UniProt
Manually annotated by BRENDA team
IBDVP2, strain P2, two-segmented double-stranded RNA virus
-
-
Manually annotated by BRENDA team
gene is part of an operon that encodes membrane proteases and is transcribed as a polycistronic mRNA in cells at different growth stages
UniProt
Manually annotated by BRENDA team
gene is part of an operon that encodes membrane proteases and is transcribed as a polycistronic mRNA in cells at different growth stages
UniProt
Manually annotated by BRENDA team
no activity in Lactobacillus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium leprae
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium tuberculosis
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus sp.
-
-
-
Manually annotated by BRENDA team
formerly Pseudomonas fluorescens, gene PFL_3985
UniProt
Manually annotated by BRENDA team
formerly Pseudomonas fluorescens, gene PFL_3985
UniProt
Manually annotated by BRENDA team
strain WCS358 and IBE4
SwissProt
Manually annotated by BRENDA team
strain WCS358 and IBE4
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
KOD1, previously called Pyrococcus kodakaraensis
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abnormal puromucyl peptides + H2O
?
show the reaction diagram
-
not in vitro
-
-
-
Abz-QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A + H2O
?
show the reaction diagram
acid resistance regulator GdE protein + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
exhibits little, if any, in vitro acyl-CoA oxidase processing activity
-
-
?
Ald4 + H2O
?
show the reaction diagram
-
i.e. potassium-activated aldehyde dehydrogenase, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
alpha-casein + H2O
?
show the reaction diagram
alpha-casein-fluorescein isothiocyanate + H2O
?
show the reaction diagram
-
-
-
?
alpha-methyl casein + H2O
?
show the reaction diagram
-
-
-
?
apoTroA + H2O
?
show the reaction diagram
ATP + H2O
phosphate + ADP
show the reaction diagram
Atp2 + H2O
?
show the reaction diagram
-
i.e. F1F0-ATP synthase subunit beta, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
bacteriophage lambda N protein + H2O
?
show the reaction diagram
-
-
-
-
?
Bacteriophage lambda N-protein + H2O
?
show the reaction diagram
-
-
-
-
-
Bacteriophage lambda protein N + H2O
Hydrolyzed bacteriophage lambda protein N
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
beta-galactosidase + H2O
?
show the reaction diagram
-
-
-
?
beta-galactosidase fragment 3-93 + H2O
?
show the reaction diagram
-
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
-
-
?
beta-galactosidase-93-titinI27 + H2O
?
show the reaction diagram
-
-
-
-
?
bovine apocytochrome P450scc + H2O
?
show the reaction diagram
-
-
-
?
calpain 10 + H2O
?
show the reaction diagram
Canavanine-containing proteins + H2O
?
show the reaction diagram
-
not in vitro
-
-
-
casein + H2O
?
show the reaction diagram
casein + H2O
hydrolyzed casein
show the reaction diagram
CcdA + H2O
?
show the reaction diagram
CcrM + H2O
?
show the reaction diagram
-
-
-
-
?
CNBr-fragments of bovine serum albumin + H2O
?
show the reaction diagram
-
less dependent on ATP hydrolysis
-
-
-
Cox4-1 + H2O
?
show the reaction diagram
-
-
-
-
?
CspD + H2O
?
show the reaction diagram
-
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 albumin + H2O
?
show the reaction diagram
-
-
-
-
-
Denatured bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
-
Denatured immunoglobulin G + H2O
?
show the reaction diagram
-
-
-
-
-
Denatured lambda Cro protein + H2O
?
show the reaction diagram
-
poor substrate, inhibits casein hydrolysis
-
-
-
DNA methyltransferase + H2O
?
show the reaction diagram
-
selectively degrades cell-cycle-regulated DNA methyltransferase thereby regulating methylation of chromosomal DNA and cellular differentiation
-
-
?
DNA-binding protein HUbeta + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
F-QLRSLNGEWRFAWFPAPEAV-Q + H2O
F-QLRSLNG + EWRFAWFPAPEAV-Q
show the reaction diagram
-
residues 4968 of betqa-galactosidase flanked by a fluorophore-quencher pair
-
-
?
FAKYWQAFRQYPRLQ + H2O
?
show the reaction diagram
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
FITC casein + H2O
?
show the reaction diagram
FITC-casein + H2O
?
show the reaction diagram
-
-
-
-
?
FlhC + H2O
?
show the reaction diagram
-
-
-
-
?
FlhD + H2O
?
show the reaction diagram
-
-
-
-
?
fluorogenic peptide S3 + H2O
?
show the reaction diagram
-
-
-
?
Fluorogenic peptides + H2O
?
show the reaction diagram
-
-
-
-
-
FRETN 89-98Abu + H2O
?
show the reaction diagram
-
peptide-based substrate containing the Y(NO2)-Abz internal fluorescence quenching pair and peptide sequence RGIT-Abu-SGRQK, no substrate for human protease ClpXP
-
-
?
FRQYPRLQGGFVWDW + H2O
?
show the reaction diagram
-
degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
FVWDWVDQSLIKYDE + H2O
?
show the reaction diagram
-
very slow degradation
-
-
?
GFP-titinI27-sul20C + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
preferred substrate
-
?
Globin + H2O
?
show the reaction diagram
Glu-Ala-Ala-Phe-4-methoxy-2-naphthylamide + H2O
Glu-Ala-Ala-Phe + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
show the reaction diagram
glutaryl-AAF-4-methoxy-beta-naphthylamide + H2O
glutaryl-AAF + 4-methoxy-beta-naphthylamine
show the reaction diagram
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
show the reaction diagram
glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
show the reaction diagram
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
show the reaction diagram
heat shock sigma factor 32 + H2O
?
show the reaction diagram
-
degraded by synergistic action of lon, Clp and HflB
-
-
?
HemA + H2O
?
show the reaction diagram
-
conditional proteolysis mediated by lon and ClpAP
-
-
?
hemoglobin A + H2O
?
show the reaction diagram
can degrade unfolded human hemoglobin A at 70C either in presence or absence of ATP, at 37C only in presence of ATP
-
?
HilA + H2O
?
show the reaction diagram
homoserine trans-succinylase + H2O
?
show the reaction diagram
-
degraded by synergistic action of lon, ClpYQ, ClpXP and/or ClpAP
-
-
?
HQWRGDFQFNISRYS + H2O
?
show the reaction diagram
-
degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
HrpR + H2O
?
show the reaction diagram
-
-
-
-
?
HSP60 + H2O
?
show the reaction diagram
-
i.e. heat shock protein 60, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
human alphaA-crystallin + H2O
?
show the reaction diagram
-
Lon recognizes conserved determinants in the folded alpha-crystallin domain itself
-
-
?
human alphaB-crystallin + H2O
?
show the reaction diagram
-
Lon recognizes conserved determinants in the folded alpha-crystallin domain itself
-
-
?
human titin + H2O
?
show the reaction diagram
-
-
-
-
?
hydroxyacyl-coenzyme A dehydrogenase + H2O
?
show the reaction diagram
-
-
-
-
?
HYPNHPLWYTLCDRY + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
IbpA + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
i.e. ketol acid reductoisomerase, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
lambda phage DNA + H2O
?
show the reaction diagram
-
-
-
?
lambda phage N protein + H2O
?
show the reaction diagram
LasI + H2O
?
show the reaction diagram
LLIRGVNRHEHHPLH + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
Lpd1 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
LTEAKHQQQFFQFRL + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
maltose-binding protein-SulA + H2O
?
show the reaction diagram
-
-
-
-
?
MarA + H2O
?
show the reaction diagram
-
-
-
-
?
MazE antitoxin + H2O
?
show the reaction diagram
-
-
-
-
?
mDHFR protein + H2O
?
show the reaction diagram
Melittin + H2O
?
show the reaction diagram
Methylglobin + H2O
?
show the reaction diagram
misfolded protein + H2O
?
show the reaction diagram
mitochondrial aconitase + H2O
?
show the reaction diagram
-
essential enzyme, particularly susceptible to oxidative damage, preferentially oxidatively modified and inactivated during ageing
-
?
mitochondrial processing peptidase alpha subunit + H2O
?
show the reaction diagram
mitochondrial processing peptidase alpha-subunit + H2O
?
show the reaction diagram
-
-
-
-
?
MPPalpha + H2O
?
show the reaction diagram
Mrp20 + H2O
?
show the reaction diagram
-
i.e. mitochondrial subunit of the large ribosomal particle, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
Mutant form of alkaline phosphatase PhoA61 + H2O
?
show the reaction diagram
-
not in vitro
-
-
-
MWRMSGIFRDVSLLH + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
N-glutaryl-alanylalanylphenylalanyl-3-methoxynaphthylamide + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
no cleavage of bond between Y and 7-amido-4-methylcoumarin
-
-
?
native aconitase + H2O
?
show the reaction diagram
-
degradation at a lower efficiency than oxidized aconitase
-
-
?
oxidized aconitase + H2O
?
show the reaction diagram
-
oxidatively modified proteins and unfolded peptides are good substrates for proteolysis by lon
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
Pancreatic polypeptide + H2O
?
show the reaction diagram
-
-
-
-
-
Parathyroid hormone + H2O
?
show the reaction diagram
-
-
-
-
-
PasA + H2O
?
show the reaction diagram
-
-
-
-
?
Pdb1 + H2O
?
show the reaction diagram
-
i.e. pyruvate dehydrogenase E1component subunit beta, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
PemI + H2O
?
show the reaction diagram
-
-
-
-
?
PMP70 + H2O
?
show the reaction diagram
-
-
-
-
?
polymerase gamma + H2O
?
show the reaction diagram
-
-
-
-
?
PpuR + H2O
?
show the reaction diagram
Pro-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O
?
show the reaction diagram
-
nonapeptide related to equine angiotensinogen
-
-
-
Proteins with highly abnormal conformation + H2O
?
show the reaction diagram
PTS1 protein + H2O
?
show the reaction diagram
-
-
-
-
?
QLRSLNGEWRFAWFPAPEAV + H2O
QLRSLNG + EWRFAWFPAPEAV
show the reaction diagram
-
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
-
-
?
Rcs + H2O
?
show the reaction diagram
-
-
-
-
?
RcsA + H2O
?
show the reaction diagram
RelB antitoxin + H2O
?
show the reaction diagram
-
-
-
-
?
ribosomal L13 protein + H2O
?
show the reaction diagram
-
-
-
-
?
ribosomal L9 protein + H2O
?
show the reaction diagram
-
-
-
-
?
ribosomal S2 protein + H2O
?
show the reaction diagram
ribulose-1,5-bisphosphate carboxylase/oxygenase + H2O
?
show the reaction diagram
RubiscoTK
-
?
RMVQRDRNHPSVIIW + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RNA
?
show the reaction diagram
-
mitochondrial lon binds preferentially to single-stranded RNA in a sequence-dependent manner
-
-
?
RWDLPLSDMYTPYVF + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWLPAMSERVTRMVQ + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWQFNRQSGFLSQMW + H2O
?
show the reaction diagram
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
S1 peptide + H2O
?
show the reaction diagram
-
decapeptide S1 containing the amino acid residues 89-98 of the bacteriophage lambdaN transcription anti-termination factor, and a fluorescence donor-acceptor pair
-
-
?
sigma factor G + H2O
?
show the reaction diagram
-
lonA
-
-
?
sigma factor H + H2O
?
show the reaction diagram
-
lonA
-
-
?
SMC protein + H2O
?
show the reaction diagram
-
lonA
-
-
?
Sod2 + H2O
?
show the reaction diagram
-
i.e. mitochondrial superoxide dismutase, displays an oxidation index greater than 1 and accumulates in mitochondria lacking pim1 activity
-
-
?
SoxS + H2O
?
show the reaction diagram
-
-
-
-
?
StAR + H2O
?
show the reaction diagram
steroidogenic acute regulatory protein + H2O
?
show the reaction diagram
StpA + H2O
?
show the reaction diagram
-
-
-
-
?
Suc-Phe-Leu-Phe-SBzl + H2O
?
show the reaction diagram
-
a N-substituted tripeptide substrate
-
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
show the reaction diagram
succinyl-FLF-4-methoxy-beta-naphthylamide + H2O
succinyl-FLF + 4-methoxy-beta-naphthylamine
show the reaction diagram
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
show the reaction diagram
succinyl-Phe-Leu-Phe-4-methoxy-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
?
SulA + H2O
?
show the reaction diagram
titin-I27CD + H2O
?
show the reaction diagram
-
variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines
-
-
?
titinI27-beta-galactosidase-93 + H2O
?
show the reaction diagram
-
-
-
-
?
titinI27-beta-galactosidase-93-titinI27 + H2O
?
show the reaction diagram
-
-
-
-
?
tmRNA-tagged protein + H2O
?
show the reaction diagram
transcription activator SoxS + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
broad specificity
-
-
Y(3-NO2)-RGIT2-aminobutyric acid-SGRQ-K(anthranilamide) + H2O
Y(3-NO2)-RGIT2-aminobutyrate + SGRQ-K(anthranilamide)
show the reaction diagram
-
-
-
-
?
Y(3-NO2)-RGITCSGRQ-K(anthranilamide) + H2O
Y(3-NO2)-RGITC + SGRQ-K(anthranilamide)
show the reaction diagram
YLEDQDMWRMSGIFR + H2O
?
show the reaction diagram
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
YRGIT-Abu-SGRQK(Bz) + H2O
?
show the reaction diagram
-
-
-
-
?
YRGITCSGRQK(benzoic acid amide) + H2O
?
show the reaction diagram
-
-
-
-
?
YRGITCSGRQK(benzoic acid) + H2O
?
show the reaction diagram
-
S2 peptide
-
-
?
YRGITCSGRQK-(dansyl) + H2O
?
show the reaction diagram
-
S4 peptide
-
-
?
YWQAFRQYPRLQGGF + H2O
?
show the reaction diagram
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
FRETN 89-98 + H2O
additional information
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Abnormal puromucyl peptides + H2O
?
show the reaction diagram
-
not in vitro
-
-
-
acid resistance regulator GdE protein + H2O
?
show the reaction diagram
-
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
-
-
?
apoTroA + H2O
?
show the reaction diagram
-
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
-
-
?
Bacteriophage lambda N-protein + H2O
?
show the reaction diagram
-
-
-
-
-
calpain 10 + H2O
?
show the reaction diagram
Canavanine-containing proteins + H2O
?
show the reaction diagram
-
not in vitro
-
-
-
LasI + H2O
?
show the reaction diagram
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
-
-
?
mitochondrial aconitase + H2O
?
show the reaction diagram
-
essential enzyme, particularly susceptible to oxidative damage, preferentially oxidatively modified and inactivated during ageing
-
?
Mutant form of alkaline phosphatase PhoA61 + H2O
?
show the reaction diagram
-
not in vitro
-
-
-
Proteins with highly abnormal conformation + H2O
?
show the reaction diagram
RcsA + H2O
?
show the reaction diagram
ribosomal S2 protein + H2O
?
show the reaction diagram
-
-
-
-
?
SulA + H2O
?
show the reaction diagram
tmRNA-tagged protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-