Sequence of ornithine decarboxylase from Lactobacillus sp. strain 30a

Hackert, Marvin L.; Carroll, Donald W.; Davidson, Lois; Kim, Soo-Ok; Momany, Cory; Vaaler, G L; Zhang, Liwen

doi:10.1128/jb.176.23.7391-7394.1994

Cited by 27 publications

(14 citation statements)

References 14 publications

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“…The inducible arginine decarboxylase gene adiA has been shown to be necessary for acid resistance of pathogenic E. coli (53). Both of the ODC genes along with adiA share a high degree of sequence similarity (21). Only the constitutive ADC has a sequence that is different from all other decarboxylases and belongs to a separate structural class (20,40).…”

Section: Resultsmentioning

confidence: 99%

Polyamines Are Essential for the Formation of Plague Biofilm

Patel¹,

Wortham²,

et al. 2006

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We provide the first evidence for a link between polyamines and biofilm levels in Yersinia pestis, the causative agent of plague. Polyamine-deficient mutants of Y. pestis were generated with a single deletion in speA or speC and a double deletion mutant. The genes speA and speC code for the biosynthetic enzymes arginine decarboxylase and ornithine decarboxylase, respectively. The level of the polyamine putrescine compared to the parental speA ؉ speC ؉ strain (KIM6؉) was depleted progressively, with the highest levels found in the Y. pestis ⌬speC mutant (55% reduction), followed by the ⌬speA mutant (95% reduction) and the ⌬speA ⌬speC mutant (>99% reduction). Spermidine, on the other hand, remained constant in the single mutants but was undetected in the double mutant. The growth rates of mutants with single deletions were not altered, while the ⌬speA ⌬speC mutant grew at 65% of the exponential growth rate of the speA ؉ speC ؉ strain. Biofilm levels were assayed by three independent measures: Congo red binding, crystal violet staining, and confocal laser scanning microscopy. The level of biofilm correlated to the level of putrescine as measured by high-performance liquid chromatography-mass spectrometry and as observed in a chemical complementation curve. Complementation of the ⌬speA ⌬speC mutant with speA showed nearly full recovery of biofilm to levels observed in the speA ؉ speC ؉ strain. Chemical complementation of the double mutant and recovery of the biofilm defect were only observed with the polyamine putrescine.

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Section: Resultsmentioning

confidence: 99%

Polyamines Are Essential for the Formation of Plague Biofilm

Patel¹,

Wortham²,

et al. 2006

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“…Orninthine decarboxylase from Lactobacillus sp. 30a has been cloned (Hackert et al 1994) and its three-dimensional structure has been determined (Momany et al 1995). Recently, the ornithine decarboxylase from a putrescine-producer strain of O. oeni has also been cloned (Marcobal et al 2004).…”

Section: Arginine and Ornithine Decarboxylasesmentioning

confidence: 98%

Amino Acid Catabolic Pathways of Lactic Acid Bacteria

Fernández

Zúñiga

2006

Critical Reviews in Microbiology

341

229

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Lactic acid bacteria (LAB) constitute a diverse group of Gram positive obligately fermentative microorganisms which include both beneficial and pathogenic strains. LAB generally have complex nutritional requirements and therefore they are usually associated with nutrient-rich environments such as animal bodies, plants and foodstuffs. Amino acids represent an important resource for LAB and their utilization serves a number of physiological roles such as intracellular pH control, generation of metabolic energy or redox power, and resistance to stress. As a consequence, the regulation of amino acid catabolism involves a wide set of both general and specific regulators and shows significant differences among LAB. Moreover, due to their fermentative metabolism, LAB amino acid catabolic pathways in some cases differ significantly from those described in best studied prokaryotic model organisms such as Escherichia coli or Bacillus subtilis. Thus, LAB amino acid catabolism constitutes an interesting case for the study of metabolic pathways. Furthermore, LAB are involved in the production of a great variety of fermented products so that the products of amino acid catabolism are also relevant for the safety and the quality of fermented products.

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“…The identity between LdcC and CadA or LDC-HA is 69%, while that between CadA and LDC-HA is 80%. LdcC shows weaker similarities to other related enzymes in E. coli such as iADC (38% identity), cODC (35%), and iODC (30%), all belonging to the group III amino acid decarboxylase (Sandmeier et al, 1994; also see Hackert et al, 1994). Although ldcC and cadA show about 68% identity in the DNA sequence over the entire coding regions, the two genes show no homology outside of the coding regions.…”

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confidence: 99%

The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme.

et al. 1997

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A gene (designated ldcC) mapped at 4.6 min on the Escherichia coli chromosome codes for a protein of 713 amino acids (aa) that shows strong similarities in both size and amino-acid sequence (69% identical residues and 85% conserved residues) to lysine decarboxylase (LDC) from E. coli (CadA, acid-inducible LDC, 715 aa) or from Hafnia alvei (739 aa). A pUC18 derivative carrying the ldcC gene conferred high LDC activities on an E. coli strain devoid of the functional cadA gene, even when the bacteria were grown under non-inducing conditions at physiological pH. Thus, the gene encodes another lysine decarboxylase, probably a constitutively expressed enzyme, the presence of which was suggested from the previous observations that low LDC activities were detectable in cadA -mutant and non-induced wild-type cells.

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Sequence of ornithine decarboxylase from Lactobacillus sp. strain 30a

Cited by 27 publications

References 14 publications

Polyamines Are Essential for the Formation of Plague Biofilm

Polyamines Are Essential for the Formation of Plague Biofilm

Amino Acid Catabolic Pathways of Lactic Acid Bacteria

The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme.

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