Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes

K. Blomqvist, M. Nikkola, P. Lehtovaara, M. L. Suihko, U. Airaksinen, K. B. Straby, J. K.C. Knowles, M. E. Penttila

Research output: Contribution to journalArticleScientificpeer-review

109 Citations (Scopus)

Abstract

The genes involved in the 2,3-butanediol pathway coding for α- acetolactate decarboxylase, α-acetolactate synthase (α-ALS), and acetoin (diacetyl) reductase were isolated from Klebsiella terrigena and shown to be located in one operon. This operon was also shown to exist in Enterobacter aerogenes. The budA gene, coding for α-acetolactate decarboxylase, gives in both organisms a protein of 259 amino acids. The amino acid similarity between these proteins is 87%. The K. terrigena genes budB and budC, coding for α-ALS and acetoin reductase, respectively, were sequenced. The 559- amino-acid-long α-ALS enzyme shows similarities to the large subunits of the Escherichia coli anabolic α-ALS enzymes encoded by the genes ilvB, ilvG, and ilvI. The K. terrigena α-ALS is also shown to complement an anabolic α- ALS-deficient E. coli strain for valine synthesis. The 243-amino-acid-long acetoin reductase has the consensus amino acid sequence for the insect-type alcohol dehydrogenase/ribitol dehydrogenase family and has extensive similarities with the N-terminal and internal regions of three known dehydrogenases and one oxidoreductase.

Original languageEnglish
Pages (from-to)1392-1404
Number of pages13
JournalJournal of Bacteriology
Volume175
Issue number5
DOIs
Publication statusPublished - 1 Jan 1993
MoE publication typeA1 Journal article-refereed

Fingerprint

butanediol dehydrogenase
Enterobacter aerogenes
acetolactate decarboxylase
Operon
Amino Acids
ribitol 2-dehydrogenase
Genes
Acetoin Dehydrogenase
Oxidoreductases
Acetolactate Synthase
Escherichia coli
Klebsiella
Alcohol Dehydrogenase
Valine
Enzymes
Insects
Amino Acid Sequence
Proteins
2,3-butylene glycol

Cite this

Blomqvist, K. ; Nikkola, M. ; Lehtovaara, P. ; Suihko, M. L. ; Airaksinen, U. ; Straby, K. B. ; Knowles, J. K.C. ; Penttila, M. E. / Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes. In: Journal of Bacteriology. 1993 ; Vol. 175, No. 5. pp. 1392-1404.
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abstract = "The genes involved in the 2,3-butanediol pathway coding for α- acetolactate decarboxylase, α-acetolactate synthase (α-ALS), and acetoin (diacetyl) reductase were isolated from Klebsiella terrigena and shown to be located in one operon. This operon was also shown to exist in Enterobacter aerogenes. The budA gene, coding for α-acetolactate decarboxylase, gives in both organisms a protein of 259 amino acids. The amino acid similarity between these proteins is 87{\%}. The K. terrigena genes budB and budC, coding for α-ALS and acetoin reductase, respectively, were sequenced. The 559- amino-acid-long α-ALS enzyme shows similarities to the large subunits of the Escherichia coli anabolic α-ALS enzymes encoded by the genes ilvB, ilvG, and ilvI. The K. terrigena α-ALS is also shown to complement an anabolic α- ALS-deficient E. coli strain for valine synthesis. The 243-amino-acid-long acetoin reductase has the consensus amino acid sequence for the insect-type alcohol dehydrogenase/ribitol dehydrogenase family and has extensive similarities with the N-terminal and internal regions of three known dehydrogenases and one oxidoreductase.",
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Blomqvist, K, Nikkola, M, Lehtovaara, P, Suihko, ML, Airaksinen, U, Straby, KB, Knowles, JKC & Penttila, ME 1993, 'Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes', Journal of Bacteriology, vol. 175, no. 5, pp. 1392-1404. https://doi.org/10.1128/jb.175.5.1392-1404.1993

Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes. / Blomqvist, K.; Nikkola, M.; Lehtovaara, P.; Suihko, M. L.; Airaksinen, U.; Straby, K. B.; Knowles, J. K.C.; Penttila, M. E.

In: Journal of Bacteriology, Vol. 175, No. 5, 01.01.1993, p. 1392-1404.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes

AU - Blomqvist, K.

AU - Nikkola, M.

AU - Lehtovaara, P.

AU - Suihko, M. L.

AU - Airaksinen, U.

AU - Straby, K. B.

AU - Knowles, J. K.C.

AU - Penttila, M. E.

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N2 - The genes involved in the 2,3-butanediol pathway coding for α- acetolactate decarboxylase, α-acetolactate synthase (α-ALS), and acetoin (diacetyl) reductase were isolated from Klebsiella terrigena and shown to be located in one operon. This operon was also shown to exist in Enterobacter aerogenes. The budA gene, coding for α-acetolactate decarboxylase, gives in both organisms a protein of 259 amino acids. The amino acid similarity between these proteins is 87%. The K. terrigena genes budB and budC, coding for α-ALS and acetoin reductase, respectively, were sequenced. The 559- amino-acid-long α-ALS enzyme shows similarities to the large subunits of the Escherichia coli anabolic α-ALS enzymes encoded by the genes ilvB, ilvG, and ilvI. The K. terrigena α-ALS is also shown to complement an anabolic α- ALS-deficient E. coli strain for valine synthesis. The 243-amino-acid-long acetoin reductase has the consensus amino acid sequence for the insect-type alcohol dehydrogenase/ribitol dehydrogenase family and has extensive similarities with the N-terminal and internal regions of three known dehydrogenases and one oxidoreductase.

AB - The genes involved in the 2,3-butanediol pathway coding for α- acetolactate decarboxylase, α-acetolactate synthase (α-ALS), and acetoin (diacetyl) reductase were isolated from Klebsiella terrigena and shown to be located in one operon. This operon was also shown to exist in Enterobacter aerogenes. The budA gene, coding for α-acetolactate decarboxylase, gives in both organisms a protein of 259 amino acids. The amino acid similarity between these proteins is 87%. The K. terrigena genes budB and budC, coding for α-ALS and acetoin reductase, respectively, were sequenced. The 559- amino-acid-long α-ALS enzyme shows similarities to the large subunits of the Escherichia coli anabolic α-ALS enzymes encoded by the genes ilvB, ilvG, and ilvI. The K. terrigena α-ALS is also shown to complement an anabolic α- ALS-deficient E. coli strain for valine synthesis. The 243-amino-acid-long acetoin reductase has the consensus amino acid sequence for the insect-type alcohol dehydrogenase/ribitol dehydrogenase family and has extensive similarities with the N-terminal and internal regions of three known dehydrogenases and one oxidoreductase.

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