Cloning of the
            <i>Lactococcus lactis adhE</i>
            Gene, Encoding a Multifunctional Alcohol Dehydrogenase, by Complementation of a Fermentative Mutant of
            <i>Escherichia coli</i>

Arnau, José; Jørgensen, Flemming; Madsen, Søren; Vrang, Astrid; Israelsen, Hans

doi:10.1128/jb.180.12.3049-3055.1998

Cited by 48 publications

(18 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…ldh is expressed 37-and 14-fold higher than ldhX and ldhB, respectively; gapB is expressed seven-fold higher than gapA; and adhE is expressed 10-fold higher than adhA. These results are consistent with those obtained with other lactococcal strains [21][22][23]. For instance, the K M value of LDH of strain ATCC 19435 for NADH (Table 1) was identical to the LDH coded by ldh (K M = 0.06 mm), but not to the one coded by ldhB (K M = 0.2 mm), as found in L. lactis strain NZ9000 and strain NZ9015 [21], respectively.…”

Section: Discussionsupporting

confidence: 89%

Inhibition kinetics of catabolic dehydrogenases by elevated moieties of ATP and ADP – implication for a new regulation mechanism in Lactococcus lactis

et al. 2010

View full text Add to dashboard Cite

ATP and ADP inhibit, in varying degrees, several dehydrogenases of the central carbon metabolism of Lactococcus lactis ATCC 19435 in vitro, i.e. glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH) and alcohol dehydrogenase (ADH). Here we demonstrate mixed inhibition for GAPDH and competitive inhibition for LDH and ADH by adenine nucleotides in single inhibition studies. The nonlinear negative co‐operativity was best modelled with Hill‐type kinetics, showing greater flexibility than the usual parabolic inhibition equation. Because these natural inhibitors are present simultaneously in the cytoplasm, multiple inhibition kinetics was determined for each dehydrogenase. For ADH and LDH, the inhibitor combinations ATP plus NAD and ADP plus NAD are indifferent to each other. Model discrimination suggested that the weak allosteric inhibition of GAPDH had no relevance when multiple inhibitors are present. Interestingly, with ADH and GAPDH the combination of ATP and ADP exhibits lower dissociation constants than with either inhibitor alone. Moreover, the concerted inhibition of ADH and GAPDH, but not of LDH, shows synergy between the two nucleotides. Similar kinetics, but without synergies, were found for horse liver and yeast ADHs, indicating that dehydrogenases can be modulated by these nucleotides in a nonlinear manner in many organisms. The action of an elevated pool of ATP and ADP may effectively inactivate lactococcal ADH, but not GAPDH and LDH, providing leverage for the observed metabolic shift to homolactic acid formation in lactococcal resting cells on maltose. Therefore, we interpret these results as a regulation mechanism contributing to readjusting the flux of ATP production in L. lactis.

show abstract

Section: Discussionsupporting

confidence: 89%

Inhibition kinetics of catabolic dehydrogenases by elevated moieties of ATP and ADP – implication for a new regulation mechanism in Lactococcus lactis

et al. 2010

View full text Add to dashboard Cite

show abstract

“…different ways to reoxidize the NADH,H 1 produced during glycolysis. The transcriptional induction of the adhE gene in L. lactis was previously reported to take place under conditions leading to medium acidification (24). AdhE overproduction in M17 also suggests that the bacterium changes its metabolism from the production of acid to neutral compounds.…”

mentioning

confidence: 83%

Proteomic characterization of the acid tolerance response inLactococcus lactis MG1363

et al. 2005

View full text Add to dashboard Cite

Exponentially growing cells of Lactococcus lactis MG1363 are able to develop an Acid Tolerance Response (ATR) when incubated at pH 5, in both rich (M17)--and chemically defined (SA)--culture media. Physiological and proteomic characterization of this adaptive response indicated that L. lactis reorganizes its metabolism in response to acid stress to a great extent and quite differently in the two media. The development of ATR was fully dependent on protein de novo synthesis in SA and only partly dependent in M17. 2D gel electrophoresis revealed a total of 90 spots induced by acidity, 80 of which were identified by mass spectrometry. Only 10 proteins (BglA, PycA, GlmS, HasC, ArgS, GatA, AtpA, ArcB, Cfa, and SodA) were overproduced in the two media. A transcriptional analysis of the corresponding genes suggested that for half of them the mode of regulation may differ in the two media. Among the protein spots upregulated during the ATR in SA but not in M17, 13 already displayed an elevated rate of synthesis in M17 at neutral pH. These proteins could play an important role in the development of the protein de novo synthesis-independent ATR observed in M17.

show abstract

“…SPBC29A3.19 has 38% overall identity to Lactococcus lactis orfb (Arnau et al , 1998) a multifunctional alcohol dehydrogenase that catalyses the reduction of acetaldehyde to ethanol during fermentation. Five other alcohol dehydrogenases have been identified in S. pombe.…”

Section: Resultsmentioning

confidence: 99%

The mating-type region ofSchizosaccharomyces pombe h?S 972: sequencing and analysis of 69 kb including the expressedmat1 locus

Xiang¹,

Wood²,

Rajandream³

et al. 2000

Yeast

View full text Add to dashboard Cite

The sequence has been determined of 68 897 bp of genomic DNA including the expressed mat1 mating‐type locus from Schizosaccharomyces pombe h−S strain 972. The DNA sequence, located on the long arm of fission yeast chromosome II and contained in two cosmid clones, was analysed to reveal one autonomously replicating sequence, two retrotransposon long terminal repeats (LTRs), one tRNAGly gene and 33 open reading frames (ORFs), of which 15 contain introns. Nine of these ORFs code for previously described genes (trt1, rpl10, rps21, nif1, sui1 (psu1), matMi, matMc, let1 and rpa4), one of which (trt1) contains 15 introns, the highest number yet recorded in a gene of S. pombe. Of the remaining 24 ORFs, sequence similarity suggests that the function of 13 of the encoded proteins may be predicted and these include four mitochondrial proteins, two transport proteins, two signalling molecules, a component of serine palmitolytransferase, a homologue of 3‐methyladenine DNA glycosylase, a multifunctional alcohol dehydrogenase, a killer toxin sensitivity factor and an acetyl transferase. Six deduced sequences appear to be related to proteins of unknown function in Saccharomyces cerevisiae or S. pombe and the remaining five are hypothetical proteins. This sequence has been submitted to the EMBL database under the following entries: SPBC23G7 (Accession No. AL035065), SPBC18E5 (AL035077) and SPBC29A3 (part) (AL022299). Copyright © 2000 John Wiley & Sons, Ltd.

show abstract

Cloning of the Lactococcus lactis adhE Gene, Encoding a Multifunctional Alcohol Dehydrogenase, by Complementation of a Fermentative Mutant of Escherichia coli

Cited by 48 publications

References 28 publications

Inhibition kinetics of catabolic dehydrogenases by elevated moieties of ATP and ADP – implication for a new regulation mechanism in Lactococcus lactis

Inhibition kinetics of catabolic dehydrogenases by elevated moieties of ATP and ADP – implication for a new regulation mechanism in Lactococcus lactis

Proteomic characterization of the acid tolerance response inLactococcus lactis MG1363

The mating-type region ofSchizosaccharomyces pombe h?S 972: sequencing and analysis of 69 kb including the expressedmat1 locus

Contact Info

Product

Resources

About