Abstract
The 3-hydroxypropionate cycle, a pathway for autotrophic carbon dioxide fixation, is reviewed with special emphasis on the biochemistry of CO2 fixing enzymes in Acidianus brierleyi, a thermophilic and acidophilic archeon. In the 3-hydroxypropionate cycle, two enzymes, acetyl-CoA carboxylase and propionyl-CoA carboxylase, catalyze CO2 fixation. It has been shown in A. brierleyi, and subsequently in Metallosphaera sedula, that acetyl-CoA carboxylase is promiscuous, acting equally well on acetyl-CoA and propionyl-CoA. The subunit structure of the acyl-CoA carboxylase was shown to be α4β4γ4. Gene cloning revealed that the genes encoding the three subunits are adjacent to each other. accC encodes the β-subunit (59 kDa subunit, biotin carboxylase subunit), accB encodes the γ-subunit (20 kDa subunit, biotin carboxyl carrier protein), and pccB encodes the α-subunit (62 kDa subunit, carboxyltransferase subunit). Sequence analyses showed that accC and accB are co-transcribed and that pccB is transcribed separately. Potential biotechnological applications for the 3-hydroxypropionate cycle are also presented.
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Ishii, M., Chuakrut, S., Arai, H. et al. Occurrence, biochemistry and possible biotechnological application of the 3-hydroxypropionate cycle. Appl Microbiol Biotechnol 64, 605–610 (2004). https://doi.org/10.1007/s00253-003-1540-z
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DOI: https://doi.org/10.1007/s00253-003-1540-z