3.1.1.3 Al3+ activates at 1 mM 682643 3.1.1.3 Ba2+ 130% activity at 2 mM 713788 3.1.1.3 Ba2+ about 7.5% activation at 1 mM 677300 3.1.1.3 Ba2+ activation, extracellular enzyme 650654 3.1.1.3 BaCl2 increases activity 80841 3.1.1.3 Ca2+ - 652764, 653692, 664923 3.1.1.3 Ca2+ 1 mM, 1.3fold stimulation 727566 3.1.1.3 Ca2+ 1.12fold activation at 1 mM, 1.36fold activation at 3 mM, 1.51fold activation at 10 mM 652591 3.1.1.3 Ca2+ 10% stimulation at 5 mM 652958 3.1.1.3 Ca2+ 104% increase in activity in the presence of 1 mM Ca2+ 690508 3.1.1.3 Ca2+ 107.2% realtive activity at 5 mM 691764 3.1.1.3 Ca2+ 14% activation of recombinant refolded enzyme at 0.1 mM, 17% inhibition at 10 mM 666825 3.1.1.3 Ca2+ 163% activity at 0.1 mM 716181 3.1.1.3 Ca2+ 183.3% activity at 1 mM 715393 3.1.1.3 Ca2+ 35% activation at 1 mM 677300 3.1.1.3 Ca2+ about 150% activity at 1-10 mM 714509 3.1.1.3 Ca2+ about 30% activation 667017 3.1.1.3 Ca2+ about 50% stimulation of activity at 1 mM 714583 3.1.1.3 Ca2+ absolutely necessary both for lipase stability in the gel and for optimum activity 715063 3.1.1.3 Ca2+ absolutely necessary both for lipase stability in the gel and for optimum activity, improves the lipase activity approximately 100fold 715063 3.1.1.3 Ca2+ activates 664795, 665175, 681355 3.1.1.3 Ca2+ activates 1.23fold at 5 mM 682611 3.1.1.3 Ca2+ activates 1.6fold, not required for expression of the enzyme, optimal at 3 mM 650429 3.1.1.3 Ca2+ activates 4.6fold at 10 mM, the Esf lipase contains a nine-residue GGXGXDXXX sequence motif in the upstream region of the C-terminal motif, known to form a parallel beta-roll structure binding Ca2+ ions 681358 3.1.1.3 Ca2+ activates at 0.1 mM 729064 3.1.1.3 Ca2+ activates at 1 mM 682643 3.1.1.3 Ca2+ activates the enantioselective hydrolysis of (R,S)-flurbiprofen ethyl ester 681482 3.1.1.3 Ca2+ activates the phospholipase A1 activity of the enzyme, overview 681263 3.1.1.3 Ca2+ activates the recombinant refolded enzyme, induces secondary structural changes, confers resistance to denaturation by guanidinium hydrochloride and to inactivation by DMSO and trifluoroethanol, Ca2+ is important for structural stability of the enzyme 666821 3.1.1.3 Ca2+ activates, recombinant enzyme 666831 3.1.1.3 Ca2+ activates, the enzyme is not dependent on Ca2+ 682646 3.1.1.3 Ca2+ activation, extracellular enzyme 650654 3.1.1.3 Ca2+ adding Ca2+ to a final concentration of 5 mM increases the activity of lipase by nearly 5fold with respect to the control 713788 3.1.1.3 Ca2+ at least 12 Ca2+ are very tightly bound to one molecule of holoenzyme, which cannot be removed by dialysis but by EDTA treatment, absolutely required for activity, cannot be substituted by other divalent metal ions 650306 3.1.1.3 Ca2+ binding involves residues D217 and D262 664815 3.1.1.3 Ca2+ both LipA and LipB contain one ion per monomeric enzyme unit, the enzyme activity is not affected by Ca2+ at 1-10 mM, 15% inhibition at 25 mM at pH 9.4-9.6 677702 3.1.1.3 Ca2+ CaCl2 increases activity 80841 3.1.1.3 Ca2+ contains one Ca2+ ion 694984 3.1.1.3 Ca2+ contains three Ca2+-binding sites in the N-catalytic domain (Ca1-Ca3), the Ca2 site is required to make PML fully active, 10 mM required for activity 694953 3.1.1.3 Ca2+ dependent on 678497 3.1.1.3 Ca2+ enhances activity 691403, 80830 3.1.1.3 Ca2+ enzyme shows Ca2+-independent thermostability and catalytic activity, enzyme contains no Ca2+-binding motif around the catalytic His156 residue 650367 3.1.1.3 Ca2+ in the absence of CaCl2, the recombinant and native enzymes retain about 10% of their activities. The maximal enzyme activity is measured at 0.5 mM CaCl2 716082 3.1.1.3 Ca2+ increases enzyme expression 650654 3.1.1.3 Ca2+ increases the thermostability and activity of both extracellular isozymes 682488 3.1.1.3 Ca2+ isozyme Lip-1 shows 114.4% relative activity in the presence of 5 mM Ca2+ 690670 3.1.1.3 Ca2+ isozyme Lip-2 shows 105.2% relative activity in the presence of 5 mM Ca2+ 690670 3.1.1.3 Ca2+ native enzyme, required for activity 650654 3.1.1.3 Ca2+ optimal concentration: 10 mM CaCl2 80839 3.1.1.3 Ca2+ required 650348, 650654 3.1.1.3 Ca2+ required for thermostability 650618 3.1.1.3 Ca2+ slight activation 665576, 682608 3.1.1.3 Ca2+ stabilizes the loop containing the catalytic His251 residue, binding site structure 665475 3.1.1.3 Ca2+ stimulates 666216 3.1.1.3 Ca2+ stimulates hydrolysis of triolein 80832 3.1.1.3 Ca2+ the catalytic activity is enhanced by Ca2+ (18%) at 30 mM and higher concentrations 692424 3.1.1.3 Ca2+ the enzyme is activated by 6 mM Ca2+ 729462 3.1.1.3 Ca2+ the reaction rate increases up to a CaCl2 concentration of 0.1 mM, declining above such value 716567 3.1.1.3 CaCl2 1.24fold stimulation at 1 mM 650654 3.1.1.3 CaCl2 no absolute requirement for CaCl2 for lipase activity (65% of maximum activity in the absence of calcium), but maximum activity is measured in the presence of 4 mM CaCl2 748394 3.1.1.3 Co2+ 112.56% increase in activity in the presence of 0.1 mM Co2+, the stimulatory effect is not observed at higher concentrations 690508 3.1.1.3 Co2+ 124% activity at 0.1 mM 716181 3.1.1.3 Co2+ activates slightly, but reduces enantioslectivity 681482 3.1.1.3 Co2+ required 650654 3.1.1.3 Co2+ the activity is enhanced more than twice at 1 mM CoCl2 713778 3.1.1.3 CoCl2 5% activation at 1 mM 663907 3.1.1.3 Cu2+ 172.5% activity at 2 mM 713788 3.1.1.3 Cu2+ 83.03% increase in activity in the presence of 1 mM Cu2+ 690508 3.1.1.3 Cu2+ activates 692905 3.1.1.3 Cu2+ no activation of recombinant refolded enzyme at 10 mM and 1 mM, 14% at 0.1 mM 666825 3.1.1.3 Cu2+ required 650654 3.1.1.3 DMSO slight activation 682608 3.1.1.3 EDTA 18% activation at 1 mM, 9% at 10 mM 663907 3.1.1.3 Fe2+ 35% activation at 1 mM 677300 3.1.1.3 Fe2+ activates, recombinant enzyme 666831 3.1.1.3 Fe3+ about 30% activation 667017 3.1.1.3 Fe3+ activates 666830 3.1.1.3 Fe3+ activates at 1 mM 682643 3.1.1.3 Fe3+ activates, recombinant enzyme 666831 3.1.1.3 Hg2+ activates at 1 mM 682643 3.1.1.3 Hg2+ highly activating 666830 3.1.1.3 Iron increases enzyme expression 650654 3.1.1.3 K+ activates 665729, 666830 3.1.1.3 K+ enhances activity 80830 3.1.1.3 K+ slight activation 652591 3.1.1.3 K+ stimulates at 6 mM, inhibits at 500 mM 666216 3.1.1.3 Li+ 106.5% relative activity at 5 mM 691764 3.1.1.3 Li+ 112% activity at 0.1 mM 716181 3.1.1.3 Li+ 140% activity at 2 mM 713788 3.1.1.3 Li+ enhances activity 80830 3.1.1.3 Mg2+ - 665672, 679289 3.1.1.3 Mg2+ 1 mM, 1.3fold stimulation 727566 3.1.1.3 Mg2+ 10% activation of recombinant refolded enzyme at 1 mM, 15% inhibition at 10 mM 666825 3.1.1.3 Mg2+ 156.25% activity at 1 mM 715393 3.1.1.3 Mg2+ 20% activation at 1 mM 650524 3.1.1.3 Mg2+ 265% activity at 1 mM 713783 3.1.1.3 Mg2+ 40% activation at 1 mM 677300 3.1.1.3 Mg2+ 46.66% increase in activity in the presence of 0.1 mM Mg2+, the stimulatory effect is not observed at higher concentrations 690508 3.1.1.3 Mg2+ acivation 653693 3.1.1.3 Mg2+ activated by Mg2+ ions (20 mM), about 140% activity at 25 mM Mg2+ 729477 3.1.1.3 Mg2+ activates 666830, 681355, 692905 3.1.1.3 Mg2+ activates at 0.1 mM 729064 3.1.1.3 Mg2+ activates at 1 mM 682643 3.1.1.3 Mg2+ activates extracellular isozyme 2 slightly 682488 3.1.1.3 Mg2+ activates, recombinant enzyme 666831 3.1.1.3 Mg2+ does not affect the enzyme activity 729462 3.1.1.3 Mg2+ enhances activity 691403 3.1.1.3 Mg2+ enhances enzyme expression 650654 3.1.1.3 Mg2+ increases enzyme expression 650654 3.1.1.3 Mg2+ required 650654 3.1.1.3 Mg2+ required for strain F-111 and KKA-5, maximal enzyme production of strain KKA-5 at 0.8 M Mg2+ 650654 3.1.1.3 Mg2+ stimulates 666216 3.1.1.3 Mg2+ the catalytic activity is enhanced by Mg2+ (12%) at 30 mM and higher concnetrations 692424 3.1.1.3 MgCl2 13% activation at 1 mM 663907 3.1.1.3 Mn2+ 113% activity at 10 mM 715063 3.1.1.3 Mn2+ 115% activity at 0.1 mM 729064 3.1.1.3 Mn2+ 143% activity at 10 mM 715063 3.1.1.3 Mn2+ 2.3fold activation at 10 mM 680279 3.1.1.3 Mn2+ 22% activation of recombinant refolded enzyme at 10 mM 666825 3.1.1.3 Mn2+ 35% activation at 1 mM 677300 3.1.1.3 Mn2+ activates slightly, but reduces enantioslectivity 681482 3.1.1.3 Mn2+ both LipA and LipB contain one ion per monomeric enzyme unit, the addition of 1 mM MnCl2 to dialyzed enzyme preparations enhances the activities at 96°C of both LipA and LipB by 3fold and increases the durations of their thermal stability at 60°C and 75°C, respectively, by 4 h 677702 3.1.1.3 MnCl2 28% activation at 1 mM 663907 3.1.1.3 Mo2+ activates 692905 3.1.1.3 additional information Ca2+ is not required to trigger the activity 692392 3.1.1.3 additional information Ca2+-concentration does not affect the enzyme production 650654 3.1.1.3 additional information enzyme activity is not affected by Mg2+, K+, Na+, Ca2+, Mn2+, NH4+, and Zn2+ up to 1.0 M 653101 3.1.1.3 additional information enzyme activity is not affected by Na+, K+, and Cu2+ at 1-10 mM 682643 3.1.1.3 additional information Fe2+ induces the enzyme expression 664866 3.1.1.3 additional information metal ions cannot activate the lipase 713808 3.1.1.3 additional information method to render ferromagnetic as well as amphipatic properties to the enzyme. The magnetic lipase dispersed in colloidal state in organic solvents exerts high enzymic activity for ester synthesis and is magnetically recovered from the reaction mixture 80831 3.1.1.3 additional information negligible stimulation by Na+ and Ca2+ at 1 mM 650524 3.1.1.3 additional information no activation with ATP alone, cAMP alone or MgCl2 alone. 57% activation with the complete system, containing ATP, cAMP and MgCl2 80856 3.1.1.3 additional information no effect by Ba2+ and Na+ 664795 3.1.1.3 additional information no effect by Cs+ 682608 3.1.1.3 additional information no effect by Na+ 666830 3.1.1.3 additional information no effect by SDS at 0.01% 663907 3.1.1.3 additional information no effects by Ca2+, K+ and Li+ 680528 3.1.1.3 additional information no metalloenzyme 650660 3.1.1.3 additional information no significant effect is found in the presence of Ca2+ and Li+ 713783 3.1.1.3 additional information not a metalloenzyme 714509 3.1.1.3 additional information not activated by Ca2+ 694933 3.1.1.3 additional information not affected by Mg2+, Ca2+, K+, Na+ 651516 3.1.1.3 additional information strain A30-1 requires a complexed medium which must contains diverse metal ions, overview 650654 3.1.1.3 additional information the enzyme activity is not affected by Ca2+ or Na+ 682616 3.1.1.3 additional information the enzyme contains a single SH group accessible to sulfhydryl reagents and not essential for activity 664191 3.1.1.3 additional information the enzyme is Ca2+ independent 692415 3.1.1.3 additional information the enzyme is no metalloenzyme, not affected by citrate, Ba2+, K+, and Mg2+ 653692 3.1.1.3 additional information the enzyme is not affected by 1 mM of K+ 677300 3.1.1.3 additional information the enzyme is not affected by Ca2+, EDTA, Mg2+, Ag+, ammmonium sulfate, NaCl, NaN3, and Cu2+ at 1-10 mM 680279 3.1.1.3 additional information the enzyme is not affected by Mg2+ at 1 mM 664645 3.1.1.3 additional information the enzyme is not influenced by Fe2+, Mn2+, and Mg2+ 713788 3.1.1.3 additional information the enzyme is not or weakly affected by Mg2+, Mn2+, Cu2+, DTT, and 2-mercaptoethanol 667017 3.1.1.3 additional information the enzyme possesses two free SH groups 664788 3.1.1.3 additional information the extracellular isozymes are not affected by SDS 682488 3.1.1.3 additional information the lipase is not dependent on Ca2+ for activation or stability 714773 3.1.1.3 Na+ - 652764 3.1.1.3 Na+ 102% activity at 1 mM 715393 3.1.1.3 Na+ 214% activity at 1 mM 713783 3.1.1.3 Na+ acivation 653693 3.1.1.3 Na+ activates 665729 3.1.1.3 Na+ activates extracellular isozyme1 slightly 682488 3.1.1.3 Na+ activation, extracellular enzyme 650654 3.1.1.3 Na+ slight activation 653692, 682608 3.1.1.3 Na+ stimulates at 6 mM, inhibits at 500 mM 666216 3.1.1.3 NaCl - 665123 3.1.1.3 NaCl no activity is detected in the absence of NaCl, optimal activity at 15% 727566 3.1.1.3 NaCl optimal concentration: 1 M 80839 3.1.1.3 NaN3 30% activation at 1 mM 663907 3.1.1.3 NH4+ acivation 653693 3.1.1.3 Ni2+ 172.5% activity at 2 mM 713788 3.1.1.3 Sn2+ no activation of recombinant refolded enzyme at 10 mM and 1 mM, 12% at 0.1 mM 666825 3.1.1.3 taurocholic acid 1.6fold stimulation at 200 mM 650654 3.1.1.3 Tween 80 9% activation at 0.01% 663907 3.1.1.3 Tween 80 increases growth and enzyme production rate at 50°C, strain -12 650654 3.1.1.3 Zn2+ 162% activity at 0.1 mM 716181 3.1.1.3 Zn2+ 41.5% increase in activity in the presence of 1 mM Zn2+, the stimulatory effect is not observed at higher concentrations 690508 3.1.1.3 Zn2+ about 30% activation 667017 3.1.1.3 Zn2+ activates 692905 3.1.1.3 Zn2+ activates extracellular isozyme 1 slightly, inhibits extracellular isozyme 2 682488 3.1.1.3 Zn2+ activates, recombinant enzyme 666831 3.1.1.3 Zn2+ contains one Zn2+ ion 694984 3.1.1.3 Zn2+ contains zinc 692392 3.1.1.3 Zn2+ Zn2+ increases the recombinant lipase activity at 1 mM to 119.22% or at 5 mM to 115.19% 715206 3.1.1.3 ZnCl2 12% activation at 1 mM 663907