Alcohol dehydrogenase is one of the most critical enzymes in the production of ethanol and butanol. Synechocystis sp. PCC 6803 is a model cyanobacterium organism that is able to produce alcohols through its autotrophic energy production system. In spite of the high potential for biofuel production by this bacteria, the structure of its alcohol dehydrogenase has not been subjected to in-depth studies. The current study was aimed to analyze the molecular model for alcohol dehydrogenase of Synechocystis sp. PCC 6803 and scrutinize the interactions of different chemicals, including substrates and coenzymes. Also, the phylogenetic tree was provided to investigate the relation between different sources. The results indicated that alcohol dehydrogenase of Synechocystis sp. PCC 6803 has a different sequence compared with other Alcohol dehydrogenases (ADHs) of cyanobacterial family members. Verification of the homology model using Ramachandran plot by PROCHECK indicated that all of the residues are in favored or allowed regions of the plot. This enzyme has two Zn ions in its structure which is very similar to the other Zn-dependent ADHs. Docking studies suggest that this enzyme could have more active sites for different substrates. In addition, this enzyme has more affinity to NADH as a cofactor and sinapaldehyde as a substrate compared with the other cofactor and substrates.

乙醇脱氢酶是乙醇和丁醇生产中最关键的酶之一。集胞藻属 PCC 6803 是一种模型蓝藻生物，能够通过其自养能源生产系统生产酒精。尽管这种细菌具有生产生物燃料的巨大潜力，但其乙醇脱氢酶的结构尚未得到深入研究。本研究旨在分析集胞藻乙醇脱氢酶的分子模型。PCC 6803 并仔细检查不同化学物质的相互作用，包括底物和辅酶。此外，还提供了系统发育树来研究不同来源之间的关系。结果表明，集胞藻的乙醇脱氢酶sp. 与蓝藻家族成员的其他醇脱氢酶 (ADH) 相比，PCC 6803 具有不同的序列。PROCHECK 使用 Ramachandran 图验证同源性模型表明所有残基都在图的有利或允许区域。这种酶的结构中有两个锌离子，这与其他依赖锌的 ADH 非常相似。对接研究表明，这种酶对于不同的底物可能有更多的活性位点。此外，与其他辅因子和底物相比，该酶对作为辅因子的 NADH 和作为底物的芥子醛具有更高的亲和力。