The activation of the ζ-class carbonic anhydrase (CAs, EC 4.2.1.1) from the diatom Thalassiosira weissflogii (TweCAζ) incorporating both Zn(II) and Cd(II) at the active site, was investigated for the first time, using a panel of natural and non-natural amino acids and amines. CdTweCAζ was completely insensitive to activation, whereas all these compounds were effective activators of the zinc-containing enzyme ZnTweCAζ, with activation constants ranging between 92 nM and 37.9 µM. The most effective ZnTweCAζ activators were l-adrenaline, 1-(2-aminoethyl)-piperazine and 4-(2-aminoethyl)-morpholine, with K_As in the range of 92–150 nM. l-His, l- and d-Tyr and some pyridyl-alkylamines, had K_As in the range of 0.62–0.98 µM, whereas l-/d-DOPA, d-Trp, histamine, serotonin and l-Asn were the next most efficient activators, with K_As in the range of 1.27–3.19 µM. The least effective activators were l-Phe (K_A of 15.4 µM) and l-Asp (K_A of 37.9 µM). This in vitro study may be useful for a more complete understanding of the activation processes of various CA enzyme families, of which the ζ-class was scarcely investigated.

首次研究了在活性位点掺入Zn（II）和Cd（II）的硅藻Thalassiosira weissflogii（TweCAζ）的ζ级碳酸酐酶（CAs，EC 4.2.1.1）的活化。天然和非天然氨基酸和胺类。CdTweCAζ对激活完全不敏感，而所有这些化合物都是含锌酶ZnTweCAζ的有效激活剂，激活常数范围为92 nM至37.9 µM。最有效的ZnTweCAζ激活剂是1-肾上腺素，1-（2-氨基乙基）-哌嗪和4-（2-氨基乙基）-吗啉，K _A范围为92–150 nM。l -His，l-和d-Tyr和一些吡啶基-烷基胺，有ķ_甲S IN 0.62-0.98μM的范围内，而升- / d -DOPA，d -Trp，组胺，血清素和升-Asn是下一个最有效的活化剂，其中K_甲s的范围为1.27-3.19 µM。的至少有效的活化剂是升-Phe（K_甲15.4μM）和升-Asp（K_甲37.9μM的）。这项体外研究对于更全面地了解各种CA酶家族的激活过程可能很有用，其中几乎没有研究过ζ类。