2010
DOI: 10.1007/s00253-010-2887-6
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Abstract: Although the de novo biosynthetic mechanism of 3-hydroxypropionic acid (3-HP) in glycerol-fermenting microorganisms is still unclear, the propanediol utilization protein (PduP) of Lactobacillus species has been suggested to be a key enzyme in this regard. To verify this hypothesis, a pduP gene from Lactobacillus reuteri was cloned and expressed, and the encoded protein was characterized. Recombinant L. reuteri PduP exhibited broad substrate specificity including 3-hydroxypropionaldehyde and utilized both NAD(+… Show more

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Cited by 47 publications
(29 citation statements)
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“…The primarily marine substrate DMSP is by far not the only source of 3-hydroxypropionate in nature, but instead, 3-hydroxypropionate is the product or intermediate of the breakdown of many substrates in a variety of environments (4,18,29,30,31,33,41). It will therefore not be surprising to also find many nonmarine organisms that will be able to derive carbon from 3-hydroxypropionate.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The primarily marine substrate DMSP is by far not the only source of 3-hydroxypropionate in nature, but instead, 3-hydroxypropionate is the product or intermediate of the breakdown of many substrates in a variety of environments (4,18,29,30,31,33,41). It will therefore not be surprising to also find many nonmarine organisms that will be able to derive carbon from 3-hydroxypropionate.…”
Section: Discussionmentioning
confidence: 99%
“…Yet another metabolic process involving 3-hydroxypropionate is the anaerobic metabolism of glycerol. There have also been reports of 3-hydroxypropionate formation by the fermentation of glycerol by lactic acid bacteria (31,41) and the anaerobic oxidation of glycerol by a sulfate-reducing bacterium (33). In summary, 3-hydroxypropionate is likely to play an important role in the overall carbon cycle as an end product or intermediate in the carbon metabolism of a variety of compounds.…”
mentioning
confidence: 99%
“…Recent studies showed that a short N-terminal sequence targets PduP to the interior of the MCP, as described above (40). Homologs of PduP from other organisms have been purified and studied biochemically (116,117). Some PduP homologs show broad enzymatic activity on various aliphatic aldehydes, including 3-hydroxypropionaldehyde (HPA), as evident from studies with the Klebsiella pneumoniae and Lactobacillus reuteri enzymes (116,117).…”
Section: Enzymes Of the 12-pd Degradative Pathwaymentioning
confidence: 99%
“…Homologs of PduP from other organisms have been purified and studied biochemically (116,117). Some PduP homologs show broad enzymatic activity on various aliphatic aldehydes, including 3-hydroxypropionaldehyde (HPA), as evident from studies with the Klebsiella pneumoniae and Lactobacillus reuteri enzymes (116,117). These homologs, which share ϳ86% amino acid sequence identity with the Salmonella PduP enzyme, are used for production of 3-hydroxypropionic acid during glycerol degradation (116,117).…”
Section: Enzymes Of the 12-pd Degradative Pathwaymentioning
confidence: 99%
“…3-HP serves as the versatile precursor of several commercially important chemicals, such as 1,3-propanediol, acrylic acid, acrylamide, acrolein [7,17], polymer [1], or as a potential nematicide [14]. Glycerol-based 3-HP biosynthesis through microbial metabolic engineering has been centered in recent years due to ample glycerol as a main by-product in the flourishing biodiesel industry [2,10].…”
Section: Introductionmentioning
confidence: 99%