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. 2011 Oct;3(4):38-54.

NAD (+) -dependent Formate Dehydrogenase from Plants

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NAD (+) -dependent Formate Dehydrogenase from Plants

A A Alekseeva et al. Acta Naturae. 2011 Oct.

Abstract

NAD(+)-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs localize in mitochondria. Formate dehydrogenase activity was first discovered as early as in 1921 in plant; however, until the past decade FDHs from plants had been considerably less studied than the enzymes from microorganisms. This review summarizes the recent results on studying the physiological role, properties, structure, and protein engineering of plant formate dehydrogenases.

Keywords: physiological role; plant formate dehydrogenase; properties; protein engineering; structure; expression;Escherichia coli.

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Figures

Fig. 1
Fig. 1
Signal sequences of plant formate dehydrogenases. Here and in Figs. 2,3 , abbreviations of enzymes are those from Table   1 . Plant enzymes are highlighted in green; fungi enzymes are highlighted in magenta; FDHs from bacteria are highlighted in blue. Specific sequences that are responsible for the transport of the enzyme to mitohondria are underlined. The residue, after which the signal peptide is eliminated, are highlighted in green italics.
Fig. 2
Fig. 2
Phylogenetic tree of N-terminal sequences for plant formate dehydrogenases.
Fig. 3
Fig. 3
Alignment of formate dehyfrogenases from different sources. Abbreviations of enzymes see in Table  1. Plant enzymes are highlighted in green; fungi enzymes are highlighted in magenta; FDHs from bacteria are highlighted in blue. Specific sequences that are responsible for transport of the enzyme to mitochondria are underlined. The numeration of residues is the same as for the FDH from Pseudomonas  sp. 101 (PseFDH). The asterisk and red font mark the conserved amino acid residue.
Fig. 4
Fig. 4
The structures of apo-(A) and holo-(B) forms of FDH from A. thaliana. Figures were obtained using PDB structures 3JTM and 3N7U, respectively. In the structure of the holo-form, the molecules of NAD + and azide ion are highlighted in magenta and red, respectively.

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