3.4.21.53	Ca2+	-	651700, 669861	
3.4.21.53	Ca2+	80-83% activity in presence of ATP compared to Mg2+	752612	
3.4.21.53	Ca2+	activation, as Ca2+-ATP	29340, 29342, 29354, 29360	
3.4.21.53	Ca2+	can replace Mg2+-ATP	29340, 29342	
3.4.21.53	Ca2+	less effective in caseinolysis	29360	
3.4.21.53	Ca2+	poor substitute for Mg2+ in ATP hydrolysis	29354, 29360	
3.4.21.53	Ca2+	slight	29354, 29360	
3.4.21.53	Ca2+	slightly less effective than Mg2+-ATP	29340	
3.4.21.53	Ca2+	with equal efficiency in peptide hydrolysis (not protein hydrolysis)	29342, 29360	
3.4.21.53	Co2+	65-70% activity in presence of ATP compared to Mg2+	752612	
3.4.21.53	Co2+	supports the hydrolysis	651700	
3.4.21.53	diphosphate	activation	29343, 29360	
3.4.21.53	diphosphate	in the presence of Mg2+, only peptide hydrolysis, not casein or serum albumin hydrolysis	29343	
3.4.21.53	diphosphate	not	29340, 29341	
3.4.21.53	Mg2+	-	29355, 651700	
3.4.21.53	Mg2+	10 mM	29350	
3.4.21.53	Mg2+	5-7 mM	29339	
3.4.21.53	Mg2+	activates, presence of free Mg2+ ions inhibits the ATPase activity of the enzyme, the effect is eliminated in the presence of the protein substrate	732906	
3.4.21.53	Mg2+	activation, Mg2+ linked oligomerization modulates the catalytic activity	650090	
3.4.21.53	Mg2+	as Mg2+-ATP	29340, 29342, 29343	
3.4.21.53	Mg2+	ATP hydrolysis and protease activity	29339, 29360	
3.4.21.53	Mg2+	enzyme needs Mg2+ ions for its activity and stability. Properties compared with ATP-dependent proteases from different sources	685483	
3.4.21.53	Mg2+	in absence, dissociation into monomers and/or dimers. In presence of Mg2+, strong and ATP-independent tendency to form hexamers	670225	
3.4.21.53	Mg2+	magnesium-dependent activation and hexamerization of the Lon AAA+ protease. Mg2+-binding site structure analysis, Mg2+ is bound in the proteolytic groove	755563	
3.4.21.53	Mg2+	Mg2+ alone much less effective	29342	
3.4.21.53	Mg2+	oligomerization is dependent on Mg2+	678475	
3.4.21.53	Mg2+	required	710400, 731174, 731724, 731814, 753673, 754159, 754600, 755340, 755444, 755478	
3.4.21.53	Mg2+	required for maximal ATP-binding and essential for proteolytic activity	29347	
3.4.21.53	Mg2+	required, activates	755391, 755395	
3.4.21.53	Mg2+	required, activates, but excess of magnesium ions has an inhibitory effect on the hydrolysis of ATP	752410	
3.4.21.53	Mg2+	requirement	29339, 29340, 29341, 29342, 29343, 29347, 29348, 29349, 29350, 29351, 29352, 29354, 29355, 29360, 29361	
3.4.21.53	Mg2+	stabilizes the enzyme complex	731835	
3.4.21.53	Mg2+	strictly dependent on, activates. Enzyme Lon-like-Ms exhibits no cleavage activity without Mg2+, regardless of the presence or absence of ATP	752612	
3.4.21.53	Mn2+	72-89% activity in presence of ATP compared to Mg2+	752612	
3.4.21.53	Mn2+	can replace Mg2+-ATP	29340, 29342, 29350	
3.4.21.53	Mn2+	only weak activity with Mn2+ alone	29342	
3.4.21.53	Mn2+	requirement, as Mn2+-ATP	29340, 29342, 29350	
3.4.21.53	Mn2+	slightly more effective than Mg2+-ATP	29340	
3.4.21.53	Mn2+	supports the hydrolysis	651700	
3.4.21.53	Mn2+	with equal efficiency in peptide hydrolysis (not protein hydrolysis)	29342	
3.4.21.53	additional information	Co2+ cannot replace Mg2+	29354	
3.4.21.53	additional information	maintenance of the holoenzyme does not require the addition of Mg2+	678475	
3.4.21.53	additional information	the enzyme activity depends on divalent cations, no activity with Zn2+	752612	
3.4.21.53	Ni2+	16-20% activity in presence of ATP compared to Mg2+	752612	
3.4.21.53	Ni2+	serves as a cofactor better than Mg2+ and Ca2+	651700	
3.4.21.53	Tetraphosphate	activation, only peptide hydrolysis, in the presence of Mg2+	29343	
3.4.21.53	Triphosphate	activation	29343, 29360	
3.4.21.53	Triphosphate	in the presence of Mg2+	29343	
3.4.21.53	Triphosphate	linear triphosphate and metaphosphate	29343	
3.4.21.53	Triphosphate	only peptide hydrolysis, not casein or serum albumin hydrolysis	29343