Biochemical and Molecular Characterization of the
            <i>Clostridium magnum</i>
            Acetoin Dehydrogenase Enzyme System

Krüger, Niels; Oppermann, Fred Bernd; Lorenzl, Heidrun; Steinbüchel, Alexander

doi:10.1128/jb.176.16.5193b.1994

Cited by 11 publications

(21 citation statements)

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“…Furthermore, as noted in the phylogenetic analysis by van Ooyen and Soppa [14], Blast searches using the S. solfataricus E1a 2 and E1b 2 gene products show that the highest sequence identities with biochemicallycharacterised proteins are with the corresponding E1 genes of the acetoin dehydrogenase complex from Clostridium magnum. In this organism, the acoX gene is similarly located between the E1b and E2 genes [15].…”

Section: Identification Of a Putative Acetoin Dehydrogenase Gene Clustermentioning

confidence: 99%

Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus

2010

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Edited by Stuart FergusonKeywords: Acetoin 2-Oxoacid dehydrogenase complex Archaea Thermophile Metabolism a b s t r a c t Like many other aerobic archaea, the hyperthermophile Sulfolobus solfataricus possesses a gene cluster encoding components of a putative 2-oxoacid dehydrogenase complex. In the current paper, we have cloned and expressed the first two genes of this cluster and demonstrate that the protein products form an a 2 b 2 hetero-tetramer possessing the catalytic activity characteristic of the first component enzyme of an acetoin dehydrogenase multienzyme complex. This represents the first report of an acetoin multienzyme complex in archaea, and contrasts with the branched-chain 2-oxoacid dehydrogenase complex activities characterised in two other archaea, Thermoplasma acidophilum and Haloferax volcanii.

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Section: Identification Of a Putative Acetoin Dehydrogenase Gene Clustermentioning

confidence: 99%

Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus

2010

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“…capricolum (odp2-mycca) (this work); M . genitalium (odp2-mycge) (MG272 from the TlGR database); B. sieurothermophilus(odp2-bacst) (Borges et al, 1990); B. subtilis (odp2-bacsu) (Wang et al, 1993), (odb2-bacsu) (Wang et al, 1993), and (odo2-bacsu) (Carlsson & Hederstedt, 1989); C. magnum (acoc-cloma) (Kruger et al, 1994); K. pneumoniue (acoc-klepn) (Deg et al, 1994); P. carbinolicus (acoc-pelca) ; P. puiida (odb2-psepu) (Burns et al, 1988); A. vinelandii(odo2-azovi) (Westphal.3~ de Kok, 1990) and (odp2-azovi) (Hanemaaijer et al, 1988); E. coli (odo2-ecoli) (Spencer et at., 1984) and (odp2-ecoli) (Guest, 1987); Staphyfococcus a u r a s (odp2-staur) (Hemila, 1991); Neurospora crassa (odptneucr) (Kreader et al, 1989); yeast (odp2-yeast) (Niu et al, 1988) and (odo2-yeast) (Repetto …”

Section: P 2 4 R a T B Mkpui:stoo Kssiopdasd O D D L A U M A N P Tunclassified

“…This protein contains an aminoterminal lipoyl domain (shown as a boxed grey area), a feature observed previously only in the DLDH proteins from A . eutrophus (Hein & Steinbuchel, 1994) and Clostridium magnum (Kruger et al, 1994). These lipoyl domains contains the characteristic conserved lysine residue (the site of lipoylation) (Mattevi et al, 1992), preceded by an aspartyl residue (residues 42 and 43).…”

Section: O O a I L C " T P A T T A O A T T M T~t A T~~a~m C -~A~~g K~mentioning

confidence: 99%

“…capricolum (dldh-mycca) (this work); A . eutrophus (dldh-alceu) (Hein & Steinbuchel, 1994); C. magnum (acol-cloma) (Kruger et al, 1994); A . laidluwii (dldh-achla) (Wallbrandt et al, 1992); M .…”

Section: L D H -R C O L I D L D H -H a A I N D1dh-hact D L D H -B mentioning

confidence: 99%

“…eutrophus (acob-alceu) (Priefert et al, 1991); P. carbinolicus (acob-pelca) ; K . pneurnoniae (acob-klepn) (Deng et al, 1994); C. magnum (acob-cloma) (Kruger et al, 1994). odpb, odbb, and acob refer to the genes encoding the P-subunits of Enzyme I of the pyruvate dehydrogenase, 2-oxoisovalerate dehydrogenase, and acetoin catabolism complexes.…”

Section: O O a I L C " T P A T T A O A T T M T~t A T~~a~m C -~A~~g K~mentioning

confidence: 99%

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Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in mycoplasma capricolum

Zhu

Peterkofsky

1996

Protein Science

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The region of the genome of Mycoplasma capricolum upstream of the portion encompassing the genes for Enzymes I and IIAg" of the phosphoeno1pyruvate:sugar phosphotransferase system (PTS) was cloned and sequenced. Examination of the sequence revealed open reading frames corresponding to numerous genes involved with the oxidation of pyruvate. The deduced gene organization is naox (encoding NADH oxidase)-lplA (encoding lipoate-protein ligase)-odpA (encoding pyruvate dehydrogenase EIa)-odpB (encoding pyruvate dehydrogenase EIP)-odp2 (encoding pyruvate dehydrogenase EI1)-dldH (encoding dihydrolipoamide dehydrogenase)-pta (encoding phosphotransacety1ase)-ack (encoding acetate kinase)-orfA (an unknown open reading frame)-kdtB-ptsl-crr. Analysis of the DNA sequence suggests that the naox and IpIA genes are part of a single operon, odpA and odpB constitute an additional operon, odp2 and dldH a third operon, andpta and ack an additional transcription unit. Phylogenetic analyses of the protein products of the odpA and odpB genes indicate that they are most similar to the corresponding proteins from Mycoplasma genitalium, Acholeplasma laidlawii, and Gram-positive organisms. The product of the odp2 gene contains a single lipoyl domain, as is the case with the corresponding proteins from M. genitalium and numerous other organisms. An evolutionary tree places the M. capricolum odp2 gene product in close relationship to the corresponding proteins from A. laidlawii and M. genitalium. The dldH gene encodes an unusual form of dihydrolipoamide dehydrogenase that contains an aminoterminal extension corresponding to a lipoyl domain, a property shared by the corresponding proteins from Alcaligenes eutrophus and Clostridium magnum. Aside from that feature, the protein is related phylogenetically to the corresponding proteins from A. laidlawii and M. genitalium. The phosphotransacetylase from M. capricolum is related most closely to the corresponding protein from M. genitalium and is distinguished easily from the enzymes from Escherichia coli and Haemophilus influenzae by the absence of the characteristic amino-terminal extension. The acetate kinase from M. capricolum is related evolutionarily to the homologous enzyme from M. genitalium. Map position comparisons of genes encoding proteins involved with pyruvate metabolism show that, whereas all the genes are clustered in M. capricolum, they are scattered in M. genitalium.

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A complete collection of single‐gene deletion mutants of Acinetobacter baylyi ADP1

Berardinis

Vallenet

Castelli

et al. 2008

Molecular Systems Biology

290

303

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We have constructed a collection of single-gene deletion mutants for all dispensable genes of the soil bacterium Acinetobacter baylyi ADP1. A total of 2594 deletion mutants were obtained, whereas 499 (16%) were not, and are therefore candidate essential genes for life on minimal medium. This essentiality data set is 88% consistent with the Escherichia coli data set inferred from the Keio mutant collection profiled for growth on minimal medium, while 80% of the orthologous genes described as essential in Pseudomonas aeruginosa are also essential in ADP1. Several strategies were undertaken to investigate ADP1 metabolism by (1) searching for discrepancies between our essentiality data and current metabolic knowledge, (2) comparing this essentiality data set to those from other organisms, (3) systematic phenotyping of the mutant collection on a variety of carbon sources (quinate, 2-3 butanediol, glucose, etc.). This collection provides a new resource for the study of gene function by forward and reverse genetic approaches and constitutes a robust experimental data source for systems biology approaches.

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Biochemical and Molecular Characterization of the Clostridium magnum Acetoin Dehydrogenase Enzyme System

Abstract: Volume 176, no. 11, p. 3225, column 2, line 9 from bottom: "-ln(2PO)/N" should read "'-(1n2)(lnP0)/N." Page 3226, Table 2, boxhead for column 4: "Wild-type/ada ogt double mutant ratio" should read "ada ogt double mutant/wildtype ratio."

Cited by 11 publications

References 0 publications

Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus

Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus

Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in mycoplasma capricolum

A complete collection of single‐gene deletion mutants of Acinetobacter baylyi ADP1

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