
pmid: 16546445
NAD+-dependent formate dehydrogenase (FDH, EC 1.2.1.2) is one of the best enzymes for the purpose of NADH regeneration in dehydrogenase-based synthesis of optically active compounds. Low operational stability and high production cost of native FDHs limit their application in commercial production of chiral compounds. The review summarizes the results on engineering of bacterial and yeast FDHs aimed at improving their chemical and thermal stability, catalytic activity, switch in coenzyme specificity from NAD+ to NADP+ and overexpression in Escherichia coli cells.
Models, Molecular, Sequence Homology, Amino Acid, Molecular Sequence Data, Coenzymes, Protein Engineering, Formate Dehydrogenases, Recombinant Proteins, Bioreactors, Yeasts, Mutation, Escherichia coli, Amino Acid Sequence
Models, Molecular, Sequence Homology, Amino Acid, Molecular Sequence Data, Coenzymes, Protein Engineering, Formate Dehydrogenases, Recombinant Proteins, Bioreactors, Yeasts, Mutation, Escherichia coli, Amino Acid Sequence
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 203 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 1% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 1% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
