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Results 1 - 10 of 13 > >>
EC Number Metals/Ions Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46K+ 30-50 mM, enhances activity 5fold. Km: 3 mM. Addition of K+ reduces monoterpene synthase activity 700662
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46K+ 500 mM are included in monoterpene synthase assay 694765
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46K+ activity is dependent on K+, the potassium binding region is defined 693257
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46K+ in presence of 50 mM potassium, the enzyme activity increases 15fold as compared to the activity in an assay devoid of potassium 716469
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46K+ MdAFS1 retains up to 12% of its activity in the absence of K+, enzyme contains K+ binding region, MdAFS1 exhibits a type II K+ response, MdAFS1 is not absolutely dependent upon M+ its unequivocal classification as type I or type II K+ activated, or that of any other terpene synthases, will not be possibl, then type I enzymes can exhibit type II kinetics and vice versa. 693257
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46K+ required 748904
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46Mg2+ 10 mM are included in farnesyl diphosphate activity assay 693257
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46Mg2+ 10 mM are included in sesquiterpene synthase assay 694765
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46Mg2+ Km: 0.248 mM, divalent cation required, preference for Mg2+. Maximal velocities with Mn2+ is about 50% of that with Mg2+ 699267
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.46Mg2+ Km: 0.7 mM 700662
Results 1 - 10 of 13 > >>