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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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.53 Endopeptidase La

General Stability

General Stability on EC 3.4.21.53 - Endopeptidase La

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
ADP and AMP bind to and stabilize the enzyme even in the absence of Mg2+
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ATP stabilizes
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ELon ist quite stable against digestion by trypsin, ADP binding does not protect. ELon binds to ADP and undergoes at least one structural change that exposes a tryptic digestion site
glycerol stabilizes
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hLon ist rapidly digested by trypsin, ADP binding does not protect
identification of four regions sensitive to chymotryptic digestion
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The pure active lon is unstable at 30°C, presumably because it cleaves itself, but degradation is prevented by 1 mM ATP or AMP-PNP. These nucleotides stabilize both the individual subunits as well as the oligomeric enzyme, suggesting that stabilization required binding but not hydrolysis of ATP.
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