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首页> 外文期刊>RSC Advances >Characterization of Cd36_03230p, a putative vanillin dehydrogenase from Candida dubliniensis
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Characterization of Cd36_03230p, a putative vanillin dehydrogenase from Candida dubliniensis

机译：来自Candida Dubliniensis的推定的香草蛋白脱氢酶CD36_03230p的表征

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摘要

A coding sequence ( CD36-03230 ) from the yeast Candida dubliniensis had been previously annotated as a vanillin dehydrogenase (VDH). The corresponding protein (CD36-03230p) was recombinantly expressed in Escherichia coli and analysed. The protein is most likely a tetramer in solution as judged by crosslinking and gel filtration experiments. CD36-03230p is an active aldehyde dehydrogenase favouring cyclic and aromatic substrates. Positive cooperativity and substrate inhibition were observed with some substrates. The redox cofactor NADP ~(+) and substrates affected the thermal stability of the protein. Interestingly, the enzyme had no detectable activity with vanillin suggesting that the annotation is incorrect. It has been previously hypothesized that a methionine residue at a key position in the active site of yeast aldehyde dehydrogenases sterically hinders cyclic substrates and restricts specificity to aliphatic aldehydes. Molecular modeling of CD36-03230p demonstrates that it has an isoleucine residue (Ile-156) at this position, further strengthening this hypothesis.
机译：来自酵母Candida Dubliniensis的编码序列（CD36-03230）预先作为香草蛋白脱氢酶（VDH）注释。相应的蛋白质（CD36-03230P）在大肠杆菌中重组表达并分析。通过交联和凝胶过滤实验判断，蛋白质最可能是溶液中的四聚体。 CD36-03230P是一种有源醛脱氢酶，有利于环状和芳族底物。用一些基材观察阳性合作和底物抑制。氧化还原辅因子NADP〜（+）和基材影响了蛋白质的热稳定性。有趣的是，酶没有Vanillin没有可检测的活性，表明注释是不正确的。先前已经假设了酵母醛脱氢酶活性位点的关键位置的蛋氨酸残留物，其隐性妨碍环状基质并限制特异性对脂族醛。 CD36-03230P的分子建模表明它具有在该位置的异亮氨酸残基（ILE-156），进一步加强了该假设。

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