D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway

Satu Kuorelahti, John Londesborough, Merja Penttilä, Peter Richard

Research output: Contribution to conferenceConference articleScientific

Abstract

There is only limited knowledge about the metabolic route for D-galacturonic acid catabolism in eukaryotic organisms; however such a metabolic route exists since many species of yeast and mould are able to utilise D-galacturonic acid. The metabolic route in bacteria is known since decades and the corresponding genes are identified. The sequencing of several eukaryotic genomes did not reveal genes which were similar to the bacterial pathway suggesting that a eukaryotic pathway exists which is different from the bacterial path. For bacteria a pathway is known consisting of 5 enzymes converting D-galacturonic acid (D-galacturonate) to pyruvate and D-glyceraldehyde 3-phosphate. The intermediate metabolites are D-tagaturonate, D-altronate, 2-dehydro 3-deoxy D-gluconate and 2-dehydro 3-deoxy D-gluconate 6-phosphate. The enzymes are uronate isomerase (EC 5.3.1.12), an NADH utilising D-tagaturonate reductase (EC 1.1.1.5), altronate dehydratase (EC 4.2.1.7), 2-dehydro 3-deoxy D-gluconatekinase (EC 2.7.1.45) and 2-dehydro 3-deoxy D-gluconate 6-phosphatealdolase (EC 4.1.2.14). We could show that in fungi a pathway exists, which is distinctly different from the bacterial pathway. In the filamentous fungus Hypocrea jecorina (Trichoderma reesei) we identified the first enzyme in this pathway, which is a D-galacturonic acid reductase. The D-galacturonic acid reductase is induced when D-galacturonic acid is the carbon source. The enzyme was purified and the amino acid sequences of tryptic fragments were obtained. We cloned the corresponding gene and expressed an active enzyme in S. cerevisiae. The enzyme converts D-galacturonic acid to L-galactonic acid in a reversible reaction. The enzyme is strictly NADPH dependent. Acknowledgements This work was founded through the Maj and Tor Nessling Foundation.
Original languageEnglish
Publication statusPublished - 2005
Event1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005) - Badajoz, Spain
Duration: 15 Mar 200518 Mar 2005

Conference

Conference1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005)
Abbreviated titleBioMicroWorld 2005
CountrySpain
CityBadajoz
Period15/03/0518/03/05

Fingerprint

galacturonic acid
enzymes
Trichoderma reesei
glyceraldehyde 3-phosphate
fungi
genes
NAD (coenzyme)
isomerases
bacteria
transferases
ligases
NADP (coenzyme)
molds (fungi)
amino acid sequences
phosphates
metabolites
yeasts
metabolism
genome
carbon

Cite this

Kuorelahti, S., Londesborough, J., Penttilä, M., & Richard, P. (2005). D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway. Paper presented at 1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005), Badajoz, Spain.
Kuorelahti, Satu ; Londesborough, John ; Penttilä, Merja ; Richard, Peter. / D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway. Paper presented at 1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005), Badajoz, Spain.
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abstract = "There is only limited knowledge about the metabolic route for D-galacturonic acid catabolism in eukaryotic organisms; however such a metabolic route exists since many species of yeast and mould are able to utilise D-galacturonic acid. The metabolic route in bacteria is known since decades and the corresponding genes are identified. The sequencing of several eukaryotic genomes did not reveal genes which were similar to the bacterial pathway suggesting that a eukaryotic pathway exists which is different from the bacterial path. For bacteria a pathway is known consisting of 5 enzymes converting D-galacturonic acid (D-galacturonate) to pyruvate and D-glyceraldehyde 3-phosphate. The intermediate metabolites are D-tagaturonate, D-altronate, 2-dehydro 3-deoxy D-gluconate and 2-dehydro 3-deoxy D-gluconate 6-phosphate. The enzymes are uronate isomerase (EC 5.3.1.12), an NADH utilising D-tagaturonate reductase (EC 1.1.1.5), altronate dehydratase (EC 4.2.1.7), 2-dehydro 3-deoxy D-gluconatekinase (EC 2.7.1.45) and 2-dehydro 3-deoxy D-gluconate 6-phosphatealdolase (EC 4.1.2.14). We could show that in fungi a pathway exists, which is distinctly different from the bacterial pathway. In the filamentous fungus Hypocrea jecorina (Trichoderma reesei) we identified the first enzyme in this pathway, which is a D-galacturonic acid reductase. The D-galacturonic acid reductase is induced when D-galacturonic acid is the carbon source. The enzyme was purified and the amino acid sequences of tryptic fragments were obtained. We cloned the corresponding gene and expressed an active enzyme in S. cerevisiae. The enzyme converts D-galacturonic acid to L-galactonic acid in a reversible reaction. The enzyme is strictly NADPH dependent. Acknowledgements This work was founded through the Maj and Tor Nessling Foundation.",
author = "Satu Kuorelahti and John Londesborough and Merja Penttil{\"a} and Peter Richard",
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Kuorelahti, S, Londesborough, J, Penttilä, M & Richard, P 2005, 'D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway' Paper presented at 1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005), Badajoz, Spain, 15/03/05 - 18/03/05, .

D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway. / Kuorelahti, Satu; Londesborough, John; Penttilä, Merja; Richard, Peter.

2005. Paper presented at 1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005), Badajoz, Spain.

Research output: Contribution to conferenceConference articleScientific

TY - CONF

T1 - D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway

AU - Kuorelahti, Satu

AU - Londesborough, John

AU - Penttilä, Merja

AU - Richard, Peter

N1 - CA2: BEL2 CA: BEL

PY - 2005

Y1 - 2005

N2 - There is only limited knowledge about the metabolic route for D-galacturonic acid catabolism in eukaryotic organisms; however such a metabolic route exists since many species of yeast and mould are able to utilise D-galacturonic acid. The metabolic route in bacteria is known since decades and the corresponding genes are identified. The sequencing of several eukaryotic genomes did not reveal genes which were similar to the bacterial pathway suggesting that a eukaryotic pathway exists which is different from the bacterial path. For bacteria a pathway is known consisting of 5 enzymes converting D-galacturonic acid (D-galacturonate) to pyruvate and D-glyceraldehyde 3-phosphate. The intermediate metabolites are D-tagaturonate, D-altronate, 2-dehydro 3-deoxy D-gluconate and 2-dehydro 3-deoxy D-gluconate 6-phosphate. The enzymes are uronate isomerase (EC 5.3.1.12), an NADH utilising D-tagaturonate reductase (EC 1.1.1.5), altronate dehydratase (EC 4.2.1.7), 2-dehydro 3-deoxy D-gluconatekinase (EC 2.7.1.45) and 2-dehydro 3-deoxy D-gluconate 6-phosphatealdolase (EC 4.1.2.14). We could show that in fungi a pathway exists, which is distinctly different from the bacterial pathway. In the filamentous fungus Hypocrea jecorina (Trichoderma reesei) we identified the first enzyme in this pathway, which is a D-galacturonic acid reductase. The D-galacturonic acid reductase is induced when D-galacturonic acid is the carbon source. The enzyme was purified and the amino acid sequences of tryptic fragments were obtained. We cloned the corresponding gene and expressed an active enzyme in S. cerevisiae. The enzyme converts D-galacturonic acid to L-galactonic acid in a reversible reaction. The enzyme is strictly NADPH dependent. Acknowledgements This work was founded through the Maj and Tor Nessling Foundation.

AB - There is only limited knowledge about the metabolic route for D-galacturonic acid catabolism in eukaryotic organisms; however such a metabolic route exists since many species of yeast and mould are able to utilise D-galacturonic acid. The metabolic route in bacteria is known since decades and the corresponding genes are identified. The sequencing of several eukaryotic genomes did not reveal genes which were similar to the bacterial pathway suggesting that a eukaryotic pathway exists which is different from the bacterial path. For bacteria a pathway is known consisting of 5 enzymes converting D-galacturonic acid (D-galacturonate) to pyruvate and D-glyceraldehyde 3-phosphate. The intermediate metabolites are D-tagaturonate, D-altronate, 2-dehydro 3-deoxy D-gluconate and 2-dehydro 3-deoxy D-gluconate 6-phosphate. The enzymes are uronate isomerase (EC 5.3.1.12), an NADH utilising D-tagaturonate reductase (EC 1.1.1.5), altronate dehydratase (EC 4.2.1.7), 2-dehydro 3-deoxy D-gluconatekinase (EC 2.7.1.45) and 2-dehydro 3-deoxy D-gluconate 6-phosphatealdolase (EC 4.1.2.14). We could show that in fungi a pathway exists, which is distinctly different from the bacterial pathway. In the filamentous fungus Hypocrea jecorina (Trichoderma reesei) we identified the first enzyme in this pathway, which is a D-galacturonic acid reductase. The D-galacturonic acid reductase is induced when D-galacturonic acid is the carbon source. The enzyme was purified and the amino acid sequences of tryptic fragments were obtained. We cloned the corresponding gene and expressed an active enzyme in S. cerevisiae. The enzyme converts D-galacturonic acid to L-galactonic acid in a reversible reaction. The enzyme is strictly NADPH dependent. Acknowledgements This work was founded through the Maj and Tor Nessling Foundation.

M3 - Conference article

ER -

Kuorelahti S, Londesborough J, Penttilä M, Richard P. D-galacturonic acid reductase is the first enzyme in the eukaryotic D-galacturonic acid catabolic pathway. 2005. Paper presented at 1st International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld-2005), Badajoz, Spain.