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Reference on EC 3.4.21.53 - Endopeptidase La

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Waxman, L.; Goldberg, A.L.
Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion
Proc. Natl. Acad. Sci. USA
79
4883-4887
1982
Escherichia coli
Manually annotated by BRENDA team
Larimore, F.S.; Waxman, L.; Goldberg, A.L.
Studies of the ATP-dependent proteolytic enzyme, protease La, from Escherichia coli
J. Biol. Chem.
257
4187-4195
1982
Escherichia coli
Manually annotated by BRENDA team
Desautels, M.; Goldberg, A.L.
Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria
J. Biol. Chem.
257
11673-11679
1982
Rattus norvegicus
Manually annotated by BRENDA team
Waxman, L.; Goldberg, A.L.
Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction
J. Biol. Chem.
260
12022-12028
1985
Escherichia coli
Manually annotated by BRENDA team
Goldberg, A.L.; Waxman, L.
The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli
J. Biol. Chem.
260
12029-12034
1985
Escherichia coli
Manually annotated by BRENDA team
Waxman, L.; Goldberg, A.L.
Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La)
Science
232
500-503
1986
Escherichia coli
Manually annotated by BRENDA team
Sonezaki, S.; Okita, K.; Oba, T.; Ishii, Y.; Kondo, A.; Kato, Y.
Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease
Appl. Microbiol. Biotechnol.
44
484-488
1995
Escherichia coli
Manually annotated by BRENDA team
Edmunds, T.; Goldberg, A.L.
Role of ATP hydrolysis in the degradation of proteins by protease La from Escherichia coli
J. Cell. Biochem.
32
187-191
1986
Escherichia coli
Manually annotated by BRENDA team
Goldberg, A.L.; Menon, A.S.; Goff, S.; Chin, D.T.
The mechanism and regulation of the ATP-dependent protease La from Escherichia coli
Biochem. Soc. Trans.
15
809-811
1987
Escherichia coli
Manually annotated by BRENDA team
Maurizi, M.R.
Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli
J. Biol. Chem.
262
2696-2703
1987
Escherichia coli
Manually annotated by BRENDA team
Menon, A.S.; Waxman, L.; Goldberg, A.L.
The energy utilized in protein breakdown by the ATP-dependent protease (La) from Escherichia coli
J. Biol. Chem.
262
722-726
1987
Escherichia coli
Manually annotated by BRENDA team
Menon, A.S.; Goldberg, A.L.
Binding of nucleotides to the ATP-dependent protease La from Escherichia coli
J. Biol. Chem.
262
14921-14928
1987
Escherichia coli
Manually annotated by BRENDA team
Menon, A.S.; Goldberg, A.L.
Protein substrates activate the ATP-dependent protease La by promoting nucleotide binding and release of bound ADP
J. Biol. Chem.
262
14929-14934
1987
Escherichia coli
Manually annotated by BRENDA team
Chin, D.T.; Goff, S.; Webster, T.; Smith, T.; Goldberg, A.L.
Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La
J. Biol. Chem.
263
11718-11728
1988
Escherichia coli
Manually annotated by BRENDA team
Baker, M.E.
Location of enzymatic and DNA-binding domains on E. coli protease La
FEBS Lett.
244
31-33
1989
Escherichia coli
Manually annotated by BRENDA team
Modha, J.; Weiner, D.P.; Cullis, P.M.; Rivett, A.J.
Effects of ATP analogues on the activity of the ion proteinase of Escherichia coli
Biochem. Soc. Trans.
18
589
1990
Escherichia coli
Manually annotated by BRENDA team
Kutejova, E.; Durcova, G.; Surovkova, E.; Kuzela, S.
Yeast mitochondrial ATP-dependent protease: purification and comparison with the homologous rat enzyme and the bacterial ATP-dependent protease La
FEBS Lett.
329
47-50
1993
Saccharomyces cerevisiae, Rattus norvegicus
Manually annotated by BRENDA team
Suzuki, C.K.; Kutejova, E.; Suda, K.
Analysis and purification of ATP-dependent mitochondrial lon protease of Saccharomyces cerevisiae
Methods Enzymol.
260
486-494
1995
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Wang, N.; Gottesman, S.; Willingham, M.C.; Gottesman, M.M.; Maurizi, M.R.
A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease
Proc. Natl. Acad. Sci. USA
90
11247-11251
1993
Brevibacillus brevis, Escherichia coli, Homo sapiens, Homo sapiens (P36776), Myxococcus xanthus
Manually annotated by BRENDA team
Fischer, H.; Glockshuber, R.
ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli
J. Biol. Chem.
268
22502-22507
1993
Escherichia coli
Manually annotated by BRENDA team
Sonezaki, S.; Konda, A.; Oba, T.; Ishii, Y.; Kato, Y.; Nakayama, H.
Overproduction and purification of Lon protease from Escherichia coli using a maltose-binding protein fusion system
Appl. Microbiol. Biotechnol.
42
313-318
1994
Escherichia coli
Manually annotated by BRENDA team
Goldberg, A.L.; Moerschell, R.P.; Chung, C.H.; Maurizi, M.R.
ATP-dependent protease La (lon) from Escherichia coli
Methods Enzymol.
244
350-375
1994
Brevibacillus brevis, Saccharomyces cerevisiae, Escherichia coli, Myxococcus xanthus, Rattus norvegicus
Manually annotated by BRENDA team
Goldberg, A.L.
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
Eur. J. Biochem.
203
9-23
1992
Bos taurus, Escherichia coli, Rattus norvegicus
Manually annotated by BRENDA team
Chung, C.H.; Goldberg, A.L.
The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La
Proc. Natl. Acad. Sci. USA
78
4931-4935
1981
Escherichia coli
Manually annotated by BRENDA team
Ito, K.; Ugata, S.; Yamagata, H.
Cloning, characterization, and inactivation of the Bacillus brevis lon gene
J. Bacteriol.
174
2281-2287
1992
Brevibacillus brevis
Manually annotated by BRENDA team
Tojo, N.; Inouye, S.; Komano, T.
Cloning and nucleotide sequence of the Myxococcus xanthus lon gene: indispensability of lon for vegetative growth
J. Bacteriol.
175
2271-2277
1993
Myxococcus xanthus
Manually annotated by BRENDA team
Oh, J.Y.; Eun, Y.M.; Yoo, S.J.; Seol, J.H.; Seong, I.S.; Lee, C.S.; Chung, C.H.
LonR9 carrying a single Glu614 to Lys mutation inhibits the ATP-dependent protease La (Lon) by forming mixed oligomeric complexes
Biochem. Biophys. Res. Commun.
250
32-35
1998
Escherichia coli, Escherichia coli RGC123
Manually annotated by BRENDA team
Roudiak, S.G.; Seth, A.; Knipfer, N.; Shrader, T.E.
The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization
Biochemistry
37
377-386
1998
Escherichia coli, Mycolicibacterium smegmatis
Manually annotated by BRENDA team
Rudyak, S.G.; Brenowitz, M.; Shrader, T.E.
Mg2+-linked oligomerization modulates the catalytic activity of the Lon (La) protease from Mycobacterium smegmatis
Biochemistry
40
9317-9323
2001
Mycolicibacterium smegmatis
Manually annotated by BRENDA team
Thomas-Wohlever, J.; Lee, I.
Kinetic characterization of the peptidase activity of Escherichia coli lon reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide and protein substrates
Biochemistry
41
9418-9425
2002
Escherichia coli
Manually annotated by BRENDA team
Wagner, I.; van Dyck, L.; Savel'ev, A.S.; Neupert, W.; Langer, T.
Autocatalytic processing of the ATP-dependent PIM1 protease: crucial function of a pro-region for sorting to mitochondria
EMBO J.
16
7317-7325
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Birghan, C.; Mundt, E.; Gorbalenya, A.E.
A non-canonical lon proteinase lacking the ATPase domain employs the ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus
EMBO J.
19
114-123
2000
Infectious bursal disease virus
Manually annotated by BRENDA team
Nishii, W.; Maruyama, T.; Matsuoka, R.; Muramatsu, T.; Takahashi, K.
The unique sites in SulA protein preferentially cleaved by ATP-dependent Lon protease from Escherichia coli
Eur. J. Biochem.
269
451-457
2002
Escherichia coli
Manually annotated by BRENDA team
Starkova, N.N.; Koroleva, E.P.; Rumsh, L.D.; Ginodman, L.M.; Rotanova, T.V.
Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme
FEBS Lett.
422
218-220
1998
Escherichia coli
Manually annotated by BRENDA team
Rasulova, F.S.; Dergousova, N.I.; Starkova, N.N.; Melnikov, E.E.; Rumsh, L.D.; Ginodman, L.M.; Rotanova, T.V.
The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity
FEBS Lett.
432
179-181
1998
Escherichia coli, Escherichia coli MH-1
Manually annotated by BRENDA team
Vasilyeva, O.V.; Kolygo, K.B.; Leonova, Y.F.; Potapenko, N.A.; Ovchinnikova, T.V.
Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis
FEBS Lett.
526
66-70
2002
Escherichia coli
Manually annotated by BRENDA team
Lu, B.; Liu, T.; Crosby, J.A.; Thomas-Wohlever, J.; Lee, I.; Suzuki, C.K.
The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals
Gene
306
45-55
2003
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
van Dyck, L.; Neupert, W.; Langer, T.
The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria
Genes Dev.
12
1515-1524
1998
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Ebel, W.; Skinner, M.M.; Dierksen, K.P.; Scott, J.M.; Trempy, J.E.
A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity
J. Bacteriol.
181
2236-2243
1999
Escherichia coli
Manually annotated by BRENDA team
Fukui, T.; Eguchi, T.; Atomi, H.; Imanaka, T.
A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins
J. Bacteriol.
184
3689-3698
2002
Thermococcus kodakarensis (Q8NKS6)
Manually annotated by BRENDA team
Botos, I.; Melnikov, E.E.; Cherry, S.; Tropea, J.E.; Khalatova, A.G.; Rasulova, F.; Dauter, Z.; Maurizi, M.R.; Rotanova, T.V.; Wlodawer, A.; Gustchina, A.
The catalytic domain of E.coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
J. Biol. Chem.
279
8140-8148
2003
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Van Dyck, L.; Pearce, D.A.; Sherman, F.
PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae
J. Biol. Chem.
269
238-242
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Teichmann, U.; van Dyck, L.; Guiard, B.; Fischer, H.; Glockshuber, R.; Neupert, W.; Langer, T.
Substitution of PIM1 protease in mitochondria by Escherichia coli Lon protease
J. Biol. Chem.
271
10137-10142
1996
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Fu, G.K.; Smith, M.J.; Markovitz, D.M.
Bacterial protease Lon is a site-specific DNA-binding protein
J. Biol. Chem.
272
534-538
1997
Escherichia coli, Escherichia coli Y1089
Manually annotated by BRENDA team
Savel'ev, A.S.; Novikova, L.A.; Kovaleva, I.E.; Luzikov, V.N.; Neupert, W.; Langer, T.
ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system
J. Biol. Chem.
273
20596-20602
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hilliard, J.J.; Simon, L.D.; Van Melderen, L.; Maurizi, M.R.
PinA inhibits ATP hydrolysis and energy-dependent protein degradation by Lon protease
J. Biol. Chem.
273
524-527
1998
Escherichia coli
Manually annotated by BRENDA team
Bota, D.A.; Davies, K.J.
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
Nat. Cell Biol.
4
674-680
2002
Homo sapiens
Manually annotated by BRENDA team
van Dijl, J.M.; Kutejova, E.; Suda, K.; Perecko, D.; Schatz, G.; Suzuki, C.K.
The ATPase and protease domains of yeast mitochondrial Lon: roles in proteolysis and respiration-dependent growth
Proc. Natl. Acad. Sci. USA
95
10584-10589
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Smith, C.K.; Baker, T.A.; Sauer, R.T.
Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
Proc. Natl. Acad. Sci. USA
96
6678-6682
1999
Escherichia coli
Manually annotated by BRENDA team
Stahlberg, H.; Kutejova, E.; Suda, K.; Wolpensinger, B.; Lustig, A.; Schatz, G.; Engel, A.; Suzuki, C.K.
Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits
Proc. Natl. Acad. Sci. USA
96
6787-6790
1999
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Suzuki, C.K.; Suda, K.; Wang, N.; Schatz, G.
Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration
Science
264
273-276
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, T.; Lu, B.; Lee, I.; Ondrovicova, G.; Kutejova, E.; Suzuki, C.K.
DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrates
J. Biol. Chem.
279
13902-13910
2004
Homo sapiens
Manually annotated by BRENDA team
Patterson, J.; Vineyard, D.; Thomas-Wohlever, J.; Behshad, R.; Burke, M.; Lee, I.
Correlation of an adenine-specific conformational change with the ATP-dependent peptidase activity of Escherichia coli Lon
Biochemistry
43
7432-7442
2004
Escherichia coli
Manually annotated by BRENDA team
Vineyard, D.; Patterson-Ward, J.; Berdis, A.J.; Lee, I.
Monitoring the timing of ATP hydrolysis with activation of peptide cleavage in Escherichia coli Lon by transient kinetics
Biochemistry
44
1671-1682
2005
Escherichia coli
Manually annotated by BRENDA team
Besche, H.; Zwickl, P.
The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site
Eur. J. Biochem.
271
4361-4365
2004
Thermoplasma acidophilum (Q9HJ89), Thermoplasma acidophilum
Manually annotated by BRENDA team
Rotanova, T.V.; Melnikov, E.E.; Khalatova, A.G.; Makhovskaya, O.V.; Botos, I.; Wlodawer, A.; Gustchina, A.
Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains
Eur. J. Biochem.
271
4865-4871
2004
Escherichia coli
Manually annotated by BRENDA team
Lee, A.Y.; Tsay, S.S.; Chen, M.Y.; Wu, S.H.
Identification of a gene encoding Lon protease from Brevibacillus thermoruber WR-249 and biochemical characterization of its thermostable recombinant enzyme
Eur. J. Biochem.
271
834-844
2004
Brevibacillus thermoruber (Q84FG5), Brevibacillus thermoruber WR-249 (Q84FG5), Brevibacillus thermoruber WR-249
Manually annotated by BRENDA team
Besche, H.; Tamura, N.; Tamura, T.; Zwickl, P.
Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum
FEBS Lett.
574
161-166
2004
Thermoplasma acidophilum
Manually annotated by BRENDA team
Nishii, W.; Suzuki, T.; Nakada, M.; Kim, Y.T.; Muramatsu, T.; Takahashi, K.
Cleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 protein
FEBS Lett.
579
6846-6850
2005
Escherichia coli
Manually annotated by BRENDA team
Nomura, K.; Kato, J.; Takiguchi, N.; Ohtake, H.; Kuroda, A.
Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli
J. Biol. Chem.
279
34406-34410
2004
Escherichia coli
Manually annotated by BRENDA team
Lee, A.Y.; Hsu, C.H.; Wu, S.H.
Functional domains of Brevibacillus thermoruber lon protease for oligomerization and DNA binding: role of N-terminal and sensor and substrate discrimination domains
J. Biol. Chem.
279
34903-34912
2004
Brevibacillus thermoruber (Q84FG5), Brevibacillus thermoruber, Brevibacillus thermoruber WR-249 (Q84FG5), Brevibacillus thermoruber WR-249
Manually annotated by BRENDA team
Im, Y.J.; Na, Y.; Kang, G.B.; Rho, S.H.; Kim, M.K.; Lee, J.H.; Chung, C.H.; Eom, S.H.
The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic dyad of Lon proteases
J. Biol. Chem.
279
53451-53457
2004
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Ondrovicova, G.; Liu, T.; Singh, K.; Tian, B.; Li, H.; Gakh, O.; Perecko, D.; Janata, J.; Granot, Z.; Orly, J.; Kutejova, E.; Suzuki, C.K.
Cleavage site selection within a folded substrate by the ATP-dependent Lon protease
J. Biol. Chem.
280
25103-25110
2005
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Vera, A.; Aris, A.; Carrio, M.; Gonzalez-Montalban, N.; Villaverde, A.
Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies
J. Biotechnol.
119
163-171
2005
Escherichia coli
Manually annotated by BRENDA team
Botos, I.; Melnikov, E.E.; Cherry, S.; Kozlov, S.; Makhovskaya, O.V.; Tropea, J.E.; Gustchina, A.; Rotanova, T.V.; Wlodawer, A.
Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases
J. Mol. Biol.
351
144-157
2005
Archaeoglobus fulgidus (O29883), Archaeoglobus fulgidus
Manually annotated by BRENDA team
Botos, I.; Melnikov, E.E.; Cherry, S.; Khalatova, A.G.; Rasulova, F.S.; Tropea, J.E.; Maurizi, M.R.; Rotanova, T.V.; Gustchina, A.; Wlodawer, A.
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution
J. Struct. Biol.
146
113-122
2004
Escherichia coli
Manually annotated by BRENDA team
Su, S.; Stephens, B.B.; Alexandre, G.; Farrand, S.K.
Lon protease of the alpha-proteobacterium Agrobacterium tumefaciens is required for normal growth, cellular morphology and full virulence
Microbiology
152
1197-1207
2006
Agrobacterium tumefaciens
Manually annotated by BRENDA team
Park, S.C.; Jia, B.; Yang, J.K.; Van, D.L.; Shao, Y.G.; Han, S.W.; Jeon, Y.J.; Chung, C.H.; Cheong, G.W.
Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli
Mol. Cell
21
129-134
2006
Escherichia coli
Manually annotated by BRENDA team
Christensen, S.K.; Maenhaut-Michel, G.; Mine, N.; Gottesman, S.; Gerdes, K.; Van Melderen, L.
Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system
Mol. Microbiol.
51
1705-1717
2004
Escherichia coli
Manually annotated by BRENDA team
Jackson, M.W.; Silva-Herzog, E.; Plano, G.V.
The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein
Mol. Microbiol.
54
1364-1378
2004
Yersinia pestis
Manually annotated by BRENDA team
Li, M.; Rasulova, F.; Melnikov, E.E.; Rotanova, T.V.; Gustchina, A.; Maurizi, M.R.; Wlodawer, A.
Crystal structure of the N-terminal domain of E. coli Lon protease
Protein Sci.
14
2895-2900
2005
Escherichia coli
Manually annotated by BRENDA team
Vasilyeva, O.V.; Martynova, N.Y.; Potapenko, N.A.; Ovchinnikova, T.V.
Isolation and characterization of fragments of the ATP-dependent protease Lon from Escherichia coli obtained by limited proteolysis
Russ. J. Bioorg. Chem.
30
306-314
2004
Escherichia coli
-
Manually annotated by BRENDA team
Ngo, J.K.; Davies, K.J.
Importance of the lon protease in mitochondrial maintenance and the significance of declining lon in aging
Ann. N. Y. Acad. Sci.
1119
78-87
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Brazas, M.D.; Breidenstein, E.B.; Overhage, J.; Hancock, R.E.
Role of lon, an ATP-dependent protease homolog, in resistance of Pseudomonas aeruginosa to ciprofloxacin
Antimicrob. Agents Chemother.
51
4276-4283
2007
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Cohn, M.T.; Ingmer, H.; Mulholland, F.; J?rgensen, K.; Wells, J.M.; Br?ndsted, L.
Contribution of conserved ATP-dependent proteases of Campylobacter jejuni to stress tolerance and virulence
Appl. Environ. Microbiol.
73
7803-7813
2007
Campylobacter jejuni, Campylobacter jejuni NCTC 11168
Manually annotated by BRENDA team
Luo, S.; McNeill, M.; Myers, T.G.; Hohman, R.J.; Levine, R.L.
Lon protease promotes survival of Escherichia coli during anaerobic glucose starvation
Arch. Microbiol.
189
181-185
2008
Escherichia coli
Manually annotated by BRENDA team
Lee, Y.Y.; Hu, H.T.; Liang, P.H.; Chak, K.F.
An E. coli lon mutant conferring partial resistance to colicin may reveal a novel role in regulating proteins involved in the translocation of colicin
Biochem. Biophys. Res. Commun.
345
1579-1585
2006
Escherichia coli, Escherichia coli K12 MG1655
Manually annotated by BRENDA team
Vineyard, D.; Zhang, X.; Lee, I.
Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease
Biochemistry
45
11432-11443
2006
Escherichia coli
Manually annotated by BRENDA team
Vineyard, D.; Patterson-Ward, J.; Lee, I.
Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease
Biochemistry
45
4602-4610
2006
Escherichia coli
Manually annotated by BRENDA team
Frase, H.; Hudak, J.; Lee, I.
Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease
Biochemistry
45
8264-8274
2006
Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Patterson-Ward, J.; Huang, J.; Lee, I.
Detection and characterization of two ATP-dependent conformational changes in proteolytically inactive Escherichia coli Lon mutants by stopped flow kinetic techniques
Biochemistry
46
13593-13605
2007
Escherichia coli
Manually annotated by BRENDA team
Frase, H.; Lee, I.
Peptidyl boronates inhibit Salmonella enterica serovar Typhimurium Lon protease by a competitive ATP-dependent mechanism
Biochemistry
46
6647-6657
2007
Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Lee, I.; Suzuki, C.K.
Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates
Biochim. Biophys. Acta
1784
727-735
2008
Saccharomyces cerevisiae, Brucella abortus, Caulobacter vibrioides, Escherichia coli, Homo sapiens, Mycolicibacterium smegmatis, Pseudomonas aeruginosa, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Thermoplasma acidophilum
Manually annotated by BRENDA team
Kuroda, A.
A polyphosphate-lon protease complex in the adaptation of Escherichia coli to amino acid starvation
Biosci. Biotechnol. Biochem.
70
325-331
2006
Escherichia coli
Manually annotated by BRENDA team
Bertani, I.; Rampioni, G.; Leoni, L.; Venturi, V.
The Pseudomonas putida Lon protease is involved in N-acyl homoserine lactone quorum sensing regulation
BMC Microbiol.
7
71
2007
Pseudomonas putida (A4Q999), Pseudomonas putida, Pseudomonas putida WCS358 (A4Q999)
Manually annotated by BRENDA team
Choy, J.S.; Aung, L.L.; Karzai, A.W.
Lon protease degrades transfer-messenger RNA-tagged proteins
J. Bacteriol.
189
6564-6571
2007
Escherichia coli
Manually annotated by BRENDA team
Omi, S.; Nakata, R.; Okamura-Ikeda, K.; Konishi, H.; Taniguchi, H.
Contribution of peroxisome-specific isoform of Lon protease in sorting PTS1 proteins to peroxisomes
J. Biochem.
143
649-660
2008
Homo sapiens
Manually annotated by BRENDA team
Lu, B.; Yadav, S.; Shah, P.G.; Liu, T.; Tian, B.; Pukszta, S.; Villaluna, N.; Kutejova, E.; Newlon, C.S.; Santos, J.H.; Suzuki, C.K.
Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance
J. Biol. Chem.
282
17363-17374
2007
Homo sapiens
Manually annotated by BRENDA team
Marr, A.K.; Overhage, J.; Bains, M.; Hancock, R.E.
The Lon protease of Pseudomonas aeruginosa is induced by aminoglycosides and is involved in biofilm formation and motility
Microbiology
153
474-482
2007
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Lee, I.; Berdis, A.J.; Suzuki, C.K.
Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies
Mol. Biosyst.
2
477-483
2006
Saccharomyces cerevisiae, Brucella abortus, Escherichia coli, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Granot, Z.; Kobiler, O.; Melamed-Book, N.; Eimerl, S.; Bahat, A.; Lu, B.; Braun, S.; Maurizi, M.R.; Suzuki, C.K.; Oppenheim, A.B.; Orly, J.
Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors
Mol. Endocrinol.
21
2164-2177
2007
Homo sapiens
Manually annotated by BRENDA team
Lan, L.; Deng, X.; Xiao, Y.; Zhou, J.M.; Tang, X.
Mutation of Lon protease differentially affects the expression of Pseudomonas syringae type III secretion system genes in rich and minimal media and reduces pathogenicity
Mol. Plant Microbe Interact.
20
682-696
2007
Pseudomonas syringae
Manually annotated by BRENDA team
Ostersetzer, O.; Kato, Y.; Adam, Z.; Sakamoto, W.
Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts
Plant Cell Physiol.
48
881-885
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Rotanova, T.V.; Botos, I.; Melnikov, E.E.; Rasulova, F.; Gustchina, A.; Maurizi, M.R.; Wlodawer, A.
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains
Protein Sci.
15
1815-1828
2006
Archaeoglobus fulgidus, Bordetella parapertussis, Brevibacillus thermoruber, Escherichia coli, Methanocaldococcus jannaschii, Mycolicibacterium smegmatis, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Tsilibaris, V.; Maenhaut-Michel, G.; Van Melderen, L.
Biological roles of the Lon ATP-dependent protease
Res. Microbiol.
157
701-713
2006
Brevibacillus brevis, Bacillus subtilis, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Homo sapiens, Myxococcus xanthus, no activity in Lactobacillus sp., no activity in Streptococcus sp., Yersinia pestis, Proteus mirabilis, Pseudomonas syringae, Salmonella enterica subsp. enterica serovar Typhimurium, Streptomyces lividans, Vibrio parahaemolyticus, no activity in Mycobacterium tuberculosis, no activity in Mycobacterium leprae
Manually annotated by BRENDA team
Makhovskaya, O.V.; Kozlov, S.; Botos, I.; Stepnov, A.A.; Andrianova, A.G.; Gushchina, A.E.; Wlodawer, A.; Melnikov, E.E.; Rotanova, T.V.
Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity
Russ. J. Bioorg. Chem.
33
610-613
2007
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O29883)
-
Manually annotated by BRENDA team
Mertova, J.; Almasiova, M.; Perecko, D.; Bilka, F.; Benesova, M.; Bezakova, L.; Psenak, M.; Kutejova, E.
ATP-dependent Lon protease from maize mitochondria - comparison with the other Lon proteases
Biologia
57
739-745
2002
Zea mays
-
Manually annotated by BRENDA team
Takaya, A.; Tabuchi, F.; Tsuchiya, H.; Isogai, E.; Yamamoto, T.
Negative regulation of quorum-sensing systems in Pseudomonas aeruginosa by ATP-dependent Lon protease
J. Bacteriol.
190
4181-4188
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9I2T9)
Manually annotated by BRENDA team
Melnikov, E.E.; Andrianova, A.G.; Morozkin, A.D.; Stepnov, A.A.; Makhovskaya, O.V.; Botos, I.; Gustchina, A.; Wlodawer, A.; Rotanova, T.V.
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments
Acta Biochim. Pol.
55
281-296
2008
Escherichia coli
Manually annotated by BRENDA team
Chir, J.L.; Liao, J.H.; Lin, Y.C.; Wu, S.H.
The N-terminal sequence after residue 247 plays an important role in structure and function of Lon protease from Brevibacillus thermoruber WR-249
Biochem. Biophys. Res. Commun.
382
762-765
2009
Brevibacillus thermoruber, Brevibacillus thermoruber WR-249
Manually annotated by BRENDA team
Patterson-Ward, J.; Tedesco, J.; Hudak, J.; Fishovitz, J.; Becker, J.; Frase, H.; McNamara, K.; Lee, I.
Utilization of synthetic peptides to evaluate the importance of substrate interaction at the proteolytic site of Escherichia coli Lon protease
Biochim. Biophys. Acta
1794
1355-1363
2009
Escherichia coli
Manually annotated by BRENDA team
Guillon, B.; Bulteau, A.L.; Wattenhofer-Donze, M.; Schmucker, S.; Friguet, B.; Puccio, H.; Drapier, J.C.; Bouton, C.
Frataxin deficiency causes upregulation of mitochondrial Lon and ClpP proteases and severe loss of mitochondrial Fe-S proteins
FEBS J.
276
1036-1047
2009
Mus musculus
Manually annotated by BRENDA team
Gur, E.; Sauer, R.T.
Recognition of misfolded proteins by Lon, a AAA(+) protease
Genes Dev.
22
2267-2277
2008
Escherichia coli
Manually annotated by BRENDA team
Simmons, L.A.; Grossman, A.D.; Walker, G.C.
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis
J. Bacteriol.
190
6758-6768
2008
Bacillus subtilis
Manually annotated by BRENDA team
Clemmer, K.M.; Rather, P.N.
The Lon protease regulates swarming motility and virulence gene expression in Proteus mirabilis
J. Med. Microbiol.
57
931-937
2008
Proteus mirabilis
Manually annotated by BRENDA team
Griffith, K.L.; Fitzpatrick, M.M.; Keen, E.F.; Wolf, R.E.
Two functions of the C-terminal domain of Escherichia coli Rob: Mediating sequestration-dispersal as a novel off-on switch for regulating Robs activity as a transcription activator and preventing degradation of Rob by Lon protease
J. Mol. Biol.
388
415-430
2009
Escherichia coli
Manually annotated by BRENDA team
Heuveling, J.; Possling, A.; Hengge, R.
A role for Lon protease in the control of the acid resistance genes of Escherichia coli
Mol. Microbiol.
69
534-547
2008
Escherichia coli
Manually annotated by BRENDA team
Stanyer, L.; Jorgensen, W.; Hori, O.; Clark, J.B.; Heales, S.J.
Inactivation of brain mitochondrial Lon protease by peroxynitrite precedes electron transport chain dysfunction
Neurochem. Int.
53
95-101
2008
Rattus norvegicus
Manually annotated by BRENDA team
Chen, S.H.; Suzuki, C.K.; Wu, S.H.
Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA
Nucleic Acids Res.
36
1273-1287
2008
Homo sapiens
Manually annotated by BRENDA team
Malik, M.; Capecci, J.; Drlica, K.
Lon protease is essential for paradoxical survival of Escherichia coli exposed to high concentrations of quinolone
Antimicrob. Agents Chemother.
53
3103-3105
2009
Escherichia coli
Manually annotated by BRENDA team
Duval, V.; Nicoloff, H.; Levy, S.B.
Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli
Antimicrob. Agents Chemother.
53
4944-4948
2009
Escherichia coli
Manually annotated by BRENDA team
Lin, Y.C.; Lee, H.C.; Wang, I.; Hsu, C.H.; Liao, J.H.; Lee, A.Y.; Chen, C.; Wu, S.H.
DNA-binding specificity of the Lon protease alpha-domain from Brevibacillus thermoruber WR-249
Biochem. Biophys. Res. Commun.
388
62-66
2009
Bacillus subtilis, Escherichia coli, Brevibacillus thermoruber, Brevibacillus thermoruber WR-249
Manually annotated by BRENDA team
Thomas, J.; Fishovitz, J.; Lee, I.
Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon protease
Biochem. Cell Biol.
88
119-128
2010
Escherichia coli
Manually annotated by BRENDA team
Liao, J.H.; Lin, Y.C.; Hsu, J.; Lee, A.Y.; Chen, T.A.; Hsu, C.H.; Chir, J.L.; Hua, K.F.; Wu, T.H.; Hong, L.J.; Yen, P.W.; Chiou, A.; Wu, S.H.
Binding and cleavage of E. coli HUbeta by the E. coli Lon protease
Biophys. J.
98
129-137
2010
Escherichia coli
Manually annotated by BRENDA team
Ngo, J.K.; Davies, K.J.
Mitochondrial Lon protease is a human stress protein
Free Radic. Biol. Med.
46
1042-1048
2009
Homo sapiens
Manually annotated by BRENDA team
Bayot, A.; Gareil, M.; Rogowska-Wrzesinska, A.; Roepstorff, P.; Friguet, B.; Bulteau, A.L.
Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1
J. Biol. Chem.
285
11445-11457
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Sakr, S.; Cirinesi, A.M.; Ullers, R.S.; Schwager, F.; Georgopoulos, C.; Genevaux, P.
Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones
J. Biol. Chem.
285
23506-23514
2010
Escherichia coli
Manually annotated by BRENDA team
Kim, S.W.; Moon, K.H.; Baik, H.S.; Kang, H.Y.; Kim, S.K.; Bahk, J.D.; Hur, J.; Lee, J.H.
Changes of physiological and biochemical properties of Salmonella enterica serovar Typhimurium by deletion of cpxR and lon genes using allelic exchange method
J. Microbiol. Methods
79
314-320
2009
Salmonella enterica
Manually annotated by BRENDA team
Ge, Z.; Karzai, A.W.
Co-evolution of multipartite interactions between an extended tmRNA tag and a robust Lon protease in Mycoplasma
Mol. Microbiol.
74
1083-1099
2009
Mycoplasma pneumoniae
Manually annotated by BRENDA team
Bissonnette, S.A.; Rivera-Rivera, I.; Sauer, R.T.; Baker, T.A.
The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease
Mol. Microbiol.
75
1539-1549
2010
Escherichia coli
Manually annotated by BRENDA team
Lingard, M.J.; Bartel, B.
Arabidopsis LON2 is necessary for peroxisomal function and sustained matrix protein import
Plant Physiol.
151
1354-1365
2009
Arabidopsis thaliana (O64948), Arabidopsis thaliana
Manually annotated by BRENDA team
Coleman, J.L.; Katona, L.I.; Kuhlow, C.; Toledo, A.; Okan, N.A.; Tokarz, R.; Benach, J.L.
Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functions
PLoS Pathog.
5
e1000676
2009
Borreliella burgdorferi (O51558), Borreliella burgdorferi (Q59185), Borreliella burgdorferi
Manually annotated by BRENDA team
Gur, E.; Sauer, R.T.
Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine
Proc. Natl. Acad. Sci. USA
106
18503-18508
2009
Escherichia coli
Manually annotated by BRENDA team
Garcia-Nafria, J.; Ondrovicova, G.; Blagova, E.; Levdikov, V.M.; Bauer, J.A.; Suzuki, C.K.; Kutejova, E.; Wilkinson, A.J.; Wilson, K.S.
Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity
Protein Sci.
19
987-999
2010
Homo sapiens (P36776), Homo sapiens
Manually annotated by BRENDA team
Fishovitz, J.; Li, M.; Frase, H.; Hudak, J.; Craig, S.; Ko, K.; Berdis, A.J.; Suzuki, C.K.; Lee, I.
Active-site-directed chemical tools for profiling mitochondrial Lon protease
ACS Chem. Biol.
6
781-788
2011
Homo sapiens
Manually annotated by BRENDA team
Li, M.; Gustchina, A.; Rasulova, F.S.; Melnikov, E.E.; Maurizi, M.R.; Rotanova, T.V.; Dauter, Z.; Wlodawer, A.
Structure of the N-terminal fragment of Escherichia coli Lon protease
Acta Crystallogr. Sect. D
66
865-873
2010
Escherichia coli (P0A9M0), Escherichia coli
Manually annotated by BRENDA team
An, Y.J.; Lee, C.R.; Supangat, S.; Lee, H.S.; Lee, J.H.; Kang, S.G.; Cha, S.S.
Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1
Acta Crystallogr. Sect. F
66
54-56
2010
Thermococcus onnurineus (B6YU74)
Manually annotated by BRENDA team
OBrien, K.M.; Schufreider, A.K.; McGill, M.A.; OBrien, K.M.; Reitter, J.N.; Mills, K.V.
Mechanism of protein splicing of the Pyrococcus abyssi lon protease intein
Biochem. Biophys. Res. Commun.
403
457-461
2010
Pyrococcus abyssi
Manually annotated by BRENDA team
Cha, S.S.; An, Y.J.; Lee, C.R.; Lee, H.S.; Kim, Y.G.; Kim, S.J.; Kwon, K.K.; De Donatis, G.M.; Lee, J.H.; Maurizi, M.R.; Kang, S.G.
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber
EMBO J.
29
3520-3530
2010
Thermococcus onnurineus (B6YU74)
Manually annotated by BRENDA team
Minami, N.; Yasuda, T.; Ishii, Y.; Fujimori, K.; Amano, F.
Regulatory role of cardiolipin in the activity of an ATP-dependent protease, Lon, from Escherichia coli
J. Biochem.
149
519-527
2011
Escherichia coli
Manually annotated by BRENDA team
Duman, R.E.; Loewe, J.
Crystal structures of Bacillus subtilis Lon protease
J. Mol. Biol.
401
653-670
2010
Bacillus subtilis (P37945), Bacillus subtilis
Manually annotated by BRENDA team
Sastre, D.E.; Paggi, R.A.; De Castro, R.E.
The Lon protease from the haloalkaliphilic archaeon Natrialba magadii is transcriptionally linked to a cluster of putative membrane proteases and displays DNA-binding activity
Microbiol. Res.
166
304-313
2011
Natrialba magadii (C5MK48), Natrialba magadii, Natrialba magadii ATCC 43099 (C5MK48)
Manually annotated by BRENDA team
Bender, T.; Lewrenz, I.; Franken, S.; Baitzel, C.; Voos, W.
Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease
Mol. Biol. Cell
22
541-554
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Yang, H.; Lee, J.; Cha, J.; Baik, H.
Negative regulation of pathogenesis in Pseudomonas syringae pv. tabaci 11528 by ATP-dependent lon protease
Mol. Cells
32
317-323
2011
Pseudomonas amygdali pv. tabaci (Q52MC0), Pseudomonas amygdali pv. tabaci, Pseudomonas amygdali pv. tabaci ATCC 11528 (Q52MC0)
Manually annotated by BRENDA team
Langklotz, S.; Narberhaus, F.
The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease
Mol. Microbiol.
80
1313-1325
2011
Escherichia coli
Manually annotated by BRENDA team
Matsushima, Y.; Goto, Y.; Kaguni, L.S.
Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)
Proc. Natl. Acad. Sci. USA
107
18410-18415
2010
Drosophila melanogaster
Manually annotated by BRENDA team
Cerletti, M.; Martinez, M.J.; Gimenez, M.I.; Sastre, D.E.; Paggi, R.A.; De Castro, R.E.
The LonB protease controls membrane lipids composition and is essential for viability in the extremophilic haloarchaeon Haloferax volcanii
Environ. Microbiol.
16
1779-1792
2014
Haloferax volcanii
Manually annotated by BRENDA team
Liao, J.H.; Ihara, K.; Kuo, C.I.; Huang, K.F.; Wakatsuki, S.; Wu, S.H.; Chang, C.I.
Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors
Acta Crystallogr. Sect. D
69
1395-1402
2013
Meiothermus taiwanensis
Manually annotated by BRENDA team
Li, J.K.; Liao, J.H.; Li, H.; Kuo, C.I.; Huang, K.F.; Yang, L.W.; Wu, S.H.; Chang, C.I.
The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones
Acta Crystallogr. Sect. D
69
1789-1797
2013
Meiothermus taiwanensis (C9DRU9), Meiothermus taiwanensis
Manually annotated by BRENDA team
Nakajima, A.; Aono, T.; Tsukada, S.; Siarot, L.; Ogawa, T.; Oyaizu, H.
Lon protease of Azorhizobium caulinodans ORS571 is required for suppression of reb gene expression
Appl. Environ. Microbiol.
78
6251-6261
2012
Azorhizobium caulinodans (A8HYF7), Azorhizobium caulinodans, Azorhizobium caulinodans ORS 571 (A8HYF7), Azorhizobium caulinodans ORS 571
Manually annotated by BRENDA team
Smith, M.; Schnellmann, R.
Mitochondrial calpain 10 is degraded by Lon protease after oxidant injury
Arch. Biochem. Biophys.
517
144-152
2012
Oryctolagus cuniculus, Oryctolagus cuniculus New Zealand White
Manually annotated by BRENDA team
Quiros, P.M.; Espanol, Y.; Acin-Perez, R.; Rodriguez, F.; Barcena, C.; Watanabe, K.; Calvo, E.; Loureiro, M.; Fernandez-Garcia, M.S.; Fueyo, A.; Vazquez, J.; Enriquez, J.A.; Lopez-Otin, C.
ATP-dependent Lon protease controls tumor bioenergetics by reprogramming mitochondrial activity
Cell Rep.
8
542-556
2014
Homo sapiens, Mus musculus (Q8CGK3)
Manually annotated by BRENDA team
Takeuchi, K.; Tsuchiya, W.; Noda, N.; Suzuki, R.; Yamazaki, T.; Haas, D.
Lon protease negatively affects GacA protein stability and expression of the Gac/Rsm signal transduction pathway in Pseudomonas protegens
Environ. Microbiol.
16
2538-2549
2014
Pseudomonas protegens (A0A2C9ETQ7), Pseudomonas protegens, Pseudomonas protegens CHA0 (A0A2C9ETQ7)
Manually annotated by BRENDA team
Goo, H.G.; Rhim, H.; Kang, S.
HtrA2/Omi influences the stability of LON protease 1 and prohibitin, proteins involved in mitochondrial homeostasis
Exp. Cell Res.
328
456-465
2014
Homo sapiens (P36776), Mus musculus (Q8CGK3), Mus musculus
Manually annotated by BRENDA team
Ambro, L.; Pevala, V.; Ondrovicova, G.; Bellova, J.; Kunova, N.; Kutejova, E.; Bauer, J.
Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities
FEBS J.
281
1784-1797
2014
Homo sapiens
Manually annotated by BRENDA team
Redelberger, D.; Genest, O.; Arabet, D.; Mejean, V.; Ilbert, M.; Iobbi-Nivol, C.
Quality control of a molybdoenzyme by the Lon protease
FEBS Lett.
587
3935-3942
2013
Escherichia coli
Manually annotated by BRENDA team
Kereiche, S.; Kovacik, L.; Pevala, V.; Ambro, L.; Bellova, J.; Kutejova, E.; Raska, I.
Three-dimensional reconstruction of the S885A mutant of human mitochondrial Lon protease
Folia Biol. (Praha)
60 Suppl 1
62-65
2014
Homo sapiens
Manually annotated by BRENDA team
Cerletti, M.; Paggi, R.A.; Guevara, C.R.; Poetsch, A.; De Castro, R.E.
Global role of the membrane protease LonB in Archaea: Potential protease targets revealed by quantitative proteome analysis of a lonB mutant in Haloferax volcanii
J. Proteomics
121
1-14
2015
Haloferax volcanii, Haloferax volcanii H26
Manually annotated by BRENDA team
Gibellini, L.; Pinti, M.; Beretti, F.; Pierri, C.L.; Onofrio, A.; Riccio, M.; Carnevale, G.; De Biasi, S.; Nasi, M.; Torelli, F.; Boraldi, F.; De Pol, A.; Cossarizza, A.
Sirtuin 3 interacts with Lon protease and regulates its acetylation status
Mitochondrion
18
76-81
2014
Homo sapiens
Manually annotated by BRENDA team
Smakowska, E.; Czarna, M.; Janska, H.
Mitochondrial ATP-dependent proteases in protection against accumulation of carbonylated proteins
Mitochondrion
19
245-251
2014
Arabidopsis thaliana
Manually annotated by BRENDA team
Wohlever, M.L.; Baker, T.A.; Sauer, R.T.
Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity
Mol. Microbiol.
91
66-78
2014
Escherichia coli
Manually annotated by BRENDA team
Breidenstein, E.B.; Janot, L.; Strehmel, J.; Fernandez, L.; Taylor, P.K.; Kukavica-Ibrulj, I.; Gellatly, S.L.; Levesque, R.C.; Overhage, J.; Hancock, R.E.
The Lon protease is essential for full virulence in Pseudomonas aeruginosa
PLoS ONE
7
e49123
2012
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Vieux, E.F.; Wohlever, M.L.; Chen, J.Z.; Sauer, R.T.; Baker, T.A.
Distinct quaternary structures of the AAA+ Lon protease control substrate degradation
Proc. Natl. Acad. Sci. USA
110
E2002-E2008
2013
Escherichia coli
Manually annotated by BRENDA team
Gur, E.; Vishkautzan, M.; Sauer, R.
Protein unfolding and degradation by the AAA+ Lon protease
Protein Sci.
21
268-278
2012
Escherichia coli
Manually annotated by BRENDA team
Andrianova, A.; Kudzhaev, A.; Serova, O.; Dergousova, N.; Rotanova, T.
Role of alpha-helical domains in functioning of ATP-dependent Lon protease of Escherichia coli
Russ. J. Bioorg. Chem.
40
620-627
2014
Escherichia coli
-
Manually annotated by BRENDA team
Kudzhaev, A.; Andrianova, A.; Dubovtseva, E.; Serova, O.; Rotanova, T.
Role of the inserted alpha-helical domain in E. coli ATP-dependent lon protease function
Acta Naturae
9
75-81
2017
Escherichia coli (P0A9M0), Escherichia coli
Manually annotated by BRENDA team
Pei, J.; Yan, J.; Jiang, Y.
Characterization of the ATP-dependent Lon-like protease in Methanobrevibacter smithii
Archaea
2016
5759765
2016
Methanobrevibacter smithii (A5UP31), Methanobrevibacter smithii, Methanobrevibacter smithii ATCC 35061 (A5UP31)
Manually annotated by BRENDA team
Pinti, M.; Gibellini, L.; Nasi, M.; De Biasi, S.; Bortolotti, C.A.; Iannone, A.; Cossarizza, A.
Emerging role of Lon protease as a master regulator of mitochondrial functions
Biochim. Biophys. Acta
1857
1300-1306
2016
Thermococcus onnurineus (B6YU74), Escherichia coli (P0A9M0), Saccharomyces cerevisiae (P36775), Homo sapiens (P36776), Mus musculus (Q8CGK3), Saccharomyces cerevisiae ATCC 204508 (P36775)
Manually annotated by BRENDA team
Sepuri, N.B.V.; Angireddy, R.; Srinivasan, S.; Guha, M.; Spear, J.; Lu, B.; Anandatheerthavarada, H.K.; Suzuki, C.K.; Avadhani, N.G.
Mitochondrial LON protease-dependent degradation of cytochrome c oxidase subunits under hypoxia and myocardial ischemia
Biochim. Biophys. Acta
1858
519-528
2017
Oryctolagus cuniculus (G1TBZ8), Oryctolagus cuniculus, Mus musculus (Q8CGK3), Mus musculus
Manually annotated by BRENDA team
Gimenez, M.; Cerletti, M.; De Castro, R.
Archaeal membrane-associated proteases Insights on Haloferax volcanii and other haloarchaea
Front. Microbiol.
6
39
2015
Thermococcus onnurineus (B6YU74), Natrialba magadii (C5MK48), Haloferax volcanii (D4GTT9), Haloferax volcanii, Archaeoglobus fulgidus (O29883), Thermococcus kodakarensis (Q8NKS6), Thermoplasma acidophilum (Q9HJ89), Natrialba magadii ATCC 43099 (C5MK48), Haloferax volcanii NCIMB 2012 (D4GTT9), Natrialba magadii NBRC 102185 (C5MK48), Archaeoglobus fulgidus NBRC 100126 (O29883), Natrialba magadii DSM 3394 (C5MK48), Archaeoglobus fulgidus ATCC 49558 (O29883), Haloferax volcanii JCM 8879 (D4GTT9), Natrialba magadii NCIMB 2190 (C5MK48), Thermoplasma acidophilum JCM 9062 (Q9HJ89), Thermoplasma acidophilum AMRC-C165 (Q9HJ89), Natrialba magadii JCM 8861 (C5MK48), Natrialba magadii CIP 104546 (C5MK48), Archaeoglobus fulgidus VC-16 (O29883), Haloferax volcanii DS2 (D4GTT9), Natrialba magadii MS3 (C5MK48), Thermoplasma acidophilum ATCC 25905 (Q9HJ89), Haloferax volcanii DSM 3757 (D4GTT9), Archaeoglobus fulgidus JCM 9628 (O29883), Thermoplasma acidophilum NBRC 15155 (Q9HJ89), Haloferax volcanii ATCC 29605 (D4GTT9), Haloferax volcanii NBRC 14742 (D4GTT9), Haloferax volcanii VKM B-1768 (D4GTT9)
Manually annotated by BRENDA team
Fishovitz, J.; Sha, Z.; Chilakala, S.; Cheng, I.; Xu, Y.; Lee, I.
Utilization of mechanistic enzymology to evaluate the significance of ADP binding to human Lon protease
Front. Mol. Biosci.
4
47
2017
Escherichia coli (P0A9M0), Escherichia coli, Homo sapiens (P36776), Homo sapiens
Manually annotated by BRENDA team
Cui, X.; Wei, Y.; Xie, X.L.; Chen, L.N.; Zhang, S.H.
Mitochondrial and peroxisomal Lon proteases play opposing roles in reproduction and growth but co-function in the normal development, stress resistance and longevity of Thermomyces lanuginosus
Fungal Genet. Biol.
103
42-54
2017
Thermomyces lanuginosus, Thermomyces lanuginosus 9W
Manually annotated by BRENDA team
Karlowicz, A.; Wegrzyn, K.; Gross, M.; Kaczynska, D.; Ropelewska, M.; Siemiatkowska, M.; Bujnicki, J.M.; Konieczny, I.
Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates
J. Biol. Chem.
292
7507-7518
2017
Escherichia coli
Manually annotated by BRENDA team
An, Y.J.; Na, J.H.; Kim, M.I.; Cha, S.S.
Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules
J. Microbiol.
53
711-717
2015
Thermococcus onnurineus
Manually annotated by BRENDA team
Zhou, X.; Teper, D.; Andrade, M.O.; Zhang, T.; Chen, S.; Song, W.Y.; Wang, N.
A phosphorylation switch on Lon protease regulates bacterial type III secretion system in host
mBio
9
e02146-17
2018
Xanthomonas citri pv. citri
Manually annotated by BRENDA team
Lee, J.H.; Ancona, V.; Zhao, Y.
Lon protease modulates virulence traits in Erwinia amylovora by direct monitoring of major regulators and indirectly through the Rcs and Gac-Csr regulatory systems
Mol. Plant Pathol.
19
827-840
2018
Erwinia amylovora (P46067), Erwinia amylovora, Erwinia amylovora Ea1189 (P46067)
Manually annotated by BRENDA team
Brown, B.L.; Vieux, E.F.; Kalastavadi, T.; Kim, S.; Chen, J.Z.; Baker, T.A.
N domain of the Lon AAA+ protease controls assembly and substrate choice
Protein Sci.
28
1239-1251
2018
Escherichia coli (P0A9M0), Escherichia coli
Manually annotated by BRENDA team
Arends, J.; Griego, M.; Thomanek, N.; Lindemann, C.; Kutscher, B.; Meyer, H.E.; Narberhaus, F.
An integrated proteomic approach uncovers novel substrates and functions of the Lon protease in Escherichia coli
Proteomics
18
e1800080
2018
Escherichia coli (P0A9M0), Escherichia coli
Manually annotated by BRENDA team
Kudzhaev, A.; Andrianova, A.; Serova, O.; Arkhipova, V.; Dubovtseva, E.; Rotanova, T.
The effect of mutations in the inserted domain of ATP-dependent Lon protease from E. coli on the enzyme function
Russ. J. Bioorg. Chem.
41
518-524
2015
Escherichia coli (P0A9M0), Escherichia coli
Manually annotated by BRENDA team
Spiridonova, V.; Kudzhaev, A.; Melnichuk, A.; Gainutdinov, A.; Andrianova, A.; Rotanova, T.
Interaction of DNA aptamers with the ATP-dependent Lon protease from Escherichia coli
Russ. J. Bioorg. Chem.
41
626-630
2015
Escherichia coli (P0A9M0)
Manually annotated by BRENDA team
Kudzhaev, A.; Dubovtseva, E.; Serova, O.; Andrianova, A.; Rotanova, T.
Effect of the deletion of the (173-280) fragment of the inserted alpha-helical domain on the functional properties of ATP-dependent Lon protease from E. coli
Russ. J. Bioorg. Chem.
44
518-527
2018
Escherichia coli (P0A9M0)
-
Manually annotated by BRENDA team
Kereiche, S.; Kovacik, L.; Bednar, J.; Pevala, V.; Kunova, N.; Ondrovicova, G.; Bauer, J.; Ambro, L.; Bellova, J.; Kutejova, E.; Raska, I.
The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease
Sci. Rep.
6
33631
2016
Homo sapiens (P36776), Homo sapiens
Manually annotated by BRENDA team
Kunova, N.; Ondrovicova, G.; Bauer, J.A.; Bellova, J.; Ambro, L.; Martinakova, L.; Kotrasova, V.; Kutejova, E.; Pevala, V.
The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes
Sci. Rep.
7
631
2017
Saccharomyces cerevisiae (P36775), Saccharomyces cerevisiae, Homo sapiens (P36776), Homo sapiens, Saccharomyces cerevisiae ATCC 204508 (P36775)
Manually annotated by BRENDA team
Sivertsson, E.M.; Jackson, S.E.; Itzhaki, L.S.
The AAA+ protease ClpXP can easily degrade a 31 and a 52-knotted protein
Sci. Rep.
9
2421
2019
Escherichia coli (P0A9M0)
Manually annotated by BRENDA team
Lin, C.C.; Su, S.C.; Su, M.Y.; Liang, P.H.; Feng, C.C.; Wu, S.H.; Chang, C.I.
Structural insights into the allosteric operation of the Lon AAA+ protease
Structure
24
667-675
2016
Meiothermus taiwanensis
Manually annotated by BRENDA team
Su, S.C.; Lin, C.C.; Tai, H.C.; Chang, M.Y.; Ho, M.R.; Babu, C.S.; Liao, J.H.; Wu, S.H.; Chang, Y.C.; Lim, C.; Chang, C.I.
Structural basis for the magnesium-dependent activation and hexamerization of the Lon AAA+ protease
Structure
24
676-686
2016
Meiothermus taiwanensis (A0A059VAZ3)
Manually annotated by BRENDA team