<scp>L</scp>-Rhamnose metabolism in <i>Pichia stipitis</i> and <i>Debaryomyces polymorphus</i>

Twerdochlib, Adriana Lacerda; Pedrosa, F. O.; Funayama, S.; Rigo, L. U.

doi:10.1139/m94-144

Cited by 30 publications

(33 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A similar pathway occurs in the yeasts Pichia stipitis and Debaryomyces polymorphus (Twerdochlib et al 1994) and is initiated by the oxidation of L-rhamnose by NAD + -dependent Lrhamnose dehydrogenase (EC 1.1.1.173), yielding either L-rhamnono-1,4-lactone or the unstable rhamnono-1,5-lactone (Rigo et al 1985;Twerdochlib et al 1994). The 1,4 lactone is hydrolyzed to L-rhamnonate by L-rhamnono-1,4-lactonase (EC 3.1.1.65) (Rigo et al 1985).…”

Section: Rhamnosementioning

confidence: 73%

“…The 1,4 lactone is hydrolyzed to L-rhamnonate by L-rhamnono-1,4-lactonase (EC 3.1.1.65) (Rigo et al 1985). The unstable 1,5-lactone has been reported to spontaneously hydrolyse to L-rhamnonate (Twerdochlib et al 1994). L-Rhamnonate is subsequently dehydrated to 2-keto-3-deoxy-L-rhamnonate by L-rhamnonate dehydratase (EC 4.2.1.90) (Rigo et al 1985;Twerdochlib et al 1994).…”

Section: Rhamnosementioning

confidence: 99%

“…L-Rhamnonate is subsequently dehydrated to 2-keto-3-deoxy-L-rhamnonate by L-rhamnonate dehydratase (EC 4.2.1.90) (Rigo et al 1985;Twerdochlib et al 1994). The product of this reaction is then cleaved into pyruvate and L-lactaldehyde by an aldolase (Rigo et al 1985;Twerdochlib et al 1994). In Pi.…”

Section: Rhamnosementioning

confidence: 99%

See 2 more Smart Citations

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Maris

Abbott

Bellissimi

et al. 2006

Antonie van Leeuwenhoek

433

276

View full text Add to dashboard Cite

Fuel ethanol production from plant biomass hydrolysates by Saccharomyces cerevisiae is of great economic and environmental significance. This paper reviews the current status with respect to alcoholic fermentation of the main plant biomass-derived monosaccharides by this yeast. Wild-type S. cerevisiae strains readily ferment glucose, mannose and fructose via the Embden-Meyerhof pathway of glycolysis, while galactose is fermented via the Leloir pathway. Construction of yeast strains that efficiently convert other potentially fermentable substrates in plant biomass hydrolysates into ethanol is a major challenge in metabolic engineering. The most abundant of these compounds is xylose. Recent metabolic and evolutionary engineering studies on S. cerevisiae strains that express a fungal xylose isomerase have enabled the rapid and efficient anaerobic fermentation of this pentose.L-Arabinose fermentation, based on the expression of a prokaryotic pathway in S. cerevisiae, has also been established, but needs further optimization before it can be considered for industrial implementation. In addition to these already investigated strategies, possible approaches for metabolic engineering of galacturonic acid and rhamnose fermentation by S. cerevisiae are discussed. An emerging and major challenge is to achieve the rapid transition from proof-of-principle experiments under 'academic' conditions (synthetic media, single substrates or simple substrate mixtures, absence of toxic inhibitors) towards efficient conversion of complex industrial substrate mixtures that contain synergistically acting inhibitors.

show abstract

Section: Rhamnosementioning

confidence: 73%

Section: Rhamnosementioning

confidence: 99%

See 1 more Smart Citation

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Maris

Abbott

Bellissimi

et al. 2006

Antonie van Leeuwenhoek

433

276

View full text Add to dashboard Cite

show abstract

“…However, for a similar enzyme, the L-erythro-3,6-dideoxy-hexulosonate (2-keto-3-deoxy-L-rhamnonate) aldolase, the equilibrium was on the substrate site. In equilibrium the substrate had about 10-fold higher concentration than pyruvate and the aldehyde (20). The K m in forward direction was 3.5 mM.…”

mentioning

confidence: 92%

“…In Aspergilli similar pathways for D-gluconate (23) and D-galactonate (24) were described in which an aldolase splits the 2-keto-3-deoxy-gluconate or -galactonate to pyruvate and D-glyceraldehyde. Also a yeast catabolic path for L-rhamnose is described where the 2-keto-3-deoxy-L-rhamnonate is split to pyruvate and L-lactaldehyde by an aldolase (20). In the eukaryotic pathways these aldolase activities were described but not the corresponding genes.…”

mentioning

confidence: 99%

The Missing Link in the Fungal D-Galacturonate Pathway

Hilditch

Berghäll

Kalkkinen

et al. 2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

The fungal path for the catabolism of D-galacturonate is only partially known. It is however distinctly different to the wellknown bacterial path. The known elements of the fungal path are D-galacturonate reductase converting D-galacturonate to L-galactonate and L-galactonate dehydratase converting L-galactonate to L-threo-3-deoxy-hexulosonate (2-keto-3-deoxy-L-galactonate). Here we describe the missing link in this pathway, an aldolase converting L-threo-3-deoxy-hexulosonate to pyruvate and L-glyceraldehyde. Fungal enzymes converting L-glyceraldehyde to glycerol have been described previously. The L-threo-3-deoxy-hexulosonate aldolase activity was induced in the mold Hypocrea jecorina (Trichoderma reesei) during growth on D-galacturonate. The enzyme was purified from this mold and a partial amino acid sequence obtained. This sequence was then used to identify the corresponding gene from the H. jecorina genome. The deletion of the gene resulted in a strain unable to grow on D-galacturonate and accumulating L-threo-3-deoxy-hexulosonate. The open reading frame was cloned from cDNA and functionally expressed in the yeast Saccharomyces cerevisiae. A histidine-tagged protein was expressed, purified, and characterized. The enzyme catalyzed reaction was reversible. With L-threo-3-deoxy-hexulosonate as substrate the K m was 3.5 mM and with pyruvate and L-glyceraldehyde the K m were 0.5 and 1.2 mM, respectively. D-Galacturonate is an important carbon source for microorganisms living on decaying plant material because D-galacturonate is the principal component of pectin. It is also of relevance in biotechnology when cheap raw materials such as pectin-rich materials like citrus peel or sugar beet pulp are to be exploited. However, knowledge about the microbial pathways for D-galacturonate catabolism is rather limited. A bacterial catabolic pathway has been described previously, whereas a fungal path is only partly known. The bacterial pathway consists of five enzymes converting D-galacturonate to pyruvate and D-glyceraldehyde-3-phosphate. The intermediate metabolites are D-ta-gaturonate, D-altronate, D-erythro-3-deoxy-hexulosonate, and D-erythro-3-deoxy-hexulosonate-6-phosphate. The enzymes in this path are uronate isomerase (EC 5.3.1.12) (1), NADHutilizing D-tagaturonate reductase (EC 1.1.1.5) (2), altronate dehydratase (EC 4.2.1.7) (3), 2-dehydro-3-deoxy-D-gluconate kinase (EC 2.7.1.45) (4), and 2-dehydro-3-deoxy-D-gluconate-6-phosphate aldolase (EC 4.1.2.14) (5). The fungal path is distinctly different. The first two steps of this pathway have been described. In the first step D-galacturonate is reduced to L-galactonate by an NADPH-coupled D-galacturonate reductase (6). In Hypocrea jecorina (Trichoderma reesei) this enzyme activity was induced when grown on D-galacturonate but the activity was absent during growth on other carbon sources. The D-galacturonate reductase gene gar1 is identified and the purified protein characterized (6). In the second step L-galactonate is converted to L-threo-3-deoxy-hexulosonate (2-keto-...

show abstract

L-Rhamnono-1,4-lactonase

Schomburg

Stephan

1998

Enzyme Handbook 15

View full text Add to dashboard Cite

L-Rhamnose metabolism in Pichia stipitis and Debaryomyces polymorphus

Cited by 30 publications

References 0 publications

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

The Missing Link in the Fungal D-Galacturonate Pathway

L-Rhamnono-1,4-lactonase

Contact Info

Product

Resources

About