The gene cluster containing four genes of the pathway for L-rhamnose catabolism in the yeast Pichia stipitis

Outi Koivistoinen (Corresponding Author), Mikko Arvas, Satu Hilditch, Andreas Petrich, Merja Penttilä, Peter Richard

Research output: Contribution to journalOther journal contributionScientificpeer-review

Abstract

For the catabolism of L-rhamnose in microorganisms two distinctly different pathways are known. One pathway has phosphorylated intermediates and an isomerase as the first enzyme and the other is an oxidative pathway without phosphorylated intermediates. In fungi only the oxidative pathway is used. In this pathway L-rhamnose is oxidised to L-rhamnono-gamma-lactone followed by a lactonase and a dehydratation reaction. The resulting 3,6-Dideoxy-L-erythro-hexulosonic acid(2-keto-3-deoxy-L-rhamnonic acid) is split by an aldolase to pyruvate and L-lactaldehyde and the L-lactaldehyde is oxidised to L-lactic acid. In the yeast Pichia stipitis the first four genes of this pathway are organized in a cluster. We show that the four genes of this cluster are upregulated on L-rhamnose but not on any other carbon source. We also characterized the L-rhamnonate dehydratase after expression in a heterologous host and identified a second gene in the P. stipitis genome coding for a 3,6-Dideoxy-L-erythro-hexulosonic acid aldolase. In eukaryotic microorganisms the genes of the cluster were found to be conserved in Pezizomycotina, in Saccharomycotina species closely related to P. stipitis and in some Basidiomycota.
Original languageEnglish
Pages (from-to)127
JournalYeast
Volume26
Issue numberS1
DOIs
Publication statusPublished - 2009
MoE publication typeNot Eligible
Event24th International Conference on Yeast Genetics and Molecular Biology - Manchester, United Kingdom
Duration: 19 Jul 200924 Jul 2009

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Rhamnose
Pichia
Multigene Family
Yeast
Fructose-Bisphosphate Aldolase
Genes
Yeasts
Hydro-Lyases
Keto Acids
Isomerases
Basidiomycota
Acids
Microorganisms
Lactones
Pyruvic Acid
Lactic Acid
Fungi
Carbon
Genome
Lactic acid

Cite this

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title = "The gene cluster containing four genes of the pathway for L-rhamnose catabolism in the yeast Pichia stipitis",
abstract = "For the catabolism of L-rhamnose in microorganisms two distinctly different pathways are known. One pathway has phosphorylated intermediates and an isomerase as the first enzyme and the other is an oxidative pathway without phosphorylated intermediates. In fungi only the oxidative pathway is used. In this pathway L-rhamnose is oxidised to L-rhamnono-gamma-lactone followed by a lactonase and a dehydratation reaction. The resulting 3,6-Dideoxy-L-erythro-hexulosonic acid(2-keto-3-deoxy-L-rhamnonic acid) is split by an aldolase to pyruvate and L-lactaldehyde and the L-lactaldehyde is oxidised to L-lactic acid. In the yeast Pichia stipitis the first four genes of this pathway are organized in a cluster. We show that the four genes of this cluster are upregulated on L-rhamnose but not on any other carbon source. We also characterized the L-rhamnonate dehydratase after expression in a heterologous host and identified a second gene in the P. stipitis genome coding for a 3,6-Dideoxy-L-erythro-hexulosonic acid aldolase. In eukaryotic microorganisms the genes of the cluster were found to be conserved in Pezizomycotina, in Saccharomycotina species closely related to P. stipitis and in some Basidiomycota.",
author = "Outi Koivistoinen and Mikko Arvas and Satu Hilditch and Andreas Petrich and Merja Penttil{\"a} and Peter Richard",
note = "Abstracts of the conference CA2: TK402 CA2: TK400",
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doi = "10.1002/yea.1689",
language = "English",
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The gene cluster containing four genes of the pathway for L-rhamnose catabolism in the yeast Pichia stipitis. / Koivistoinen, Outi (Corresponding Author); Arvas, Mikko; Hilditch, Satu; Petrich, Andreas; Penttilä, Merja; Richard, Peter.

In: Yeast, Vol. 26, No. S1, 2009, p. 127.

Research output: Contribution to journalOther journal contributionScientificpeer-review

TY - JOUR

T1 - The gene cluster containing four genes of the pathway for L-rhamnose catabolism in the yeast Pichia stipitis

AU - Koivistoinen, Outi

AU - Arvas, Mikko

AU - Hilditch, Satu

AU - Petrich, Andreas

AU - Penttilä, Merja

AU - Richard, Peter

N1 - Abstracts of the conference CA2: TK402 CA2: TK400

PY - 2009

Y1 - 2009

N2 - For the catabolism of L-rhamnose in microorganisms two distinctly different pathways are known. One pathway has phosphorylated intermediates and an isomerase as the first enzyme and the other is an oxidative pathway without phosphorylated intermediates. In fungi only the oxidative pathway is used. In this pathway L-rhamnose is oxidised to L-rhamnono-gamma-lactone followed by a lactonase and a dehydratation reaction. The resulting 3,6-Dideoxy-L-erythro-hexulosonic acid(2-keto-3-deoxy-L-rhamnonic acid) is split by an aldolase to pyruvate and L-lactaldehyde and the L-lactaldehyde is oxidised to L-lactic acid. In the yeast Pichia stipitis the first four genes of this pathway are organized in a cluster. We show that the four genes of this cluster are upregulated on L-rhamnose but not on any other carbon source. We also characterized the L-rhamnonate dehydratase after expression in a heterologous host and identified a second gene in the P. stipitis genome coding for a 3,6-Dideoxy-L-erythro-hexulosonic acid aldolase. In eukaryotic microorganisms the genes of the cluster were found to be conserved in Pezizomycotina, in Saccharomycotina species closely related to P. stipitis and in some Basidiomycota.

AB - For the catabolism of L-rhamnose in microorganisms two distinctly different pathways are known. One pathway has phosphorylated intermediates and an isomerase as the first enzyme and the other is an oxidative pathway without phosphorylated intermediates. In fungi only the oxidative pathway is used. In this pathway L-rhamnose is oxidised to L-rhamnono-gamma-lactone followed by a lactonase and a dehydratation reaction. The resulting 3,6-Dideoxy-L-erythro-hexulosonic acid(2-keto-3-deoxy-L-rhamnonic acid) is split by an aldolase to pyruvate and L-lactaldehyde and the L-lactaldehyde is oxidised to L-lactic acid. In the yeast Pichia stipitis the first four genes of this pathway are organized in a cluster. We show that the four genes of this cluster are upregulated on L-rhamnose but not on any other carbon source. We also characterized the L-rhamnonate dehydratase after expression in a heterologous host and identified a second gene in the P. stipitis genome coding for a 3,6-Dideoxy-L-erythro-hexulosonic acid aldolase. In eukaryotic microorganisms the genes of the cluster were found to be conserved in Pezizomycotina, in Saccharomycotina species closely related to P. stipitis and in some Basidiomycota.

U2 - 10.1002/yea.1689

DO - 10.1002/yea.1689

M3 - Other journal contribution

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JO - Yeast

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