Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic properties

Recsei, Paul A.; Snell, Esmond E.

doi:10.1021/bi00809a003

Cited by 94 publications

(71 citation statements)

References 9 publications

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“…First, to maintain pH homeostasis under mild acid shock, bacteria induce a change in the composition of outer-membrane proteins and in cell-surface hydrophobicity (Dilworth & Glenn, 1999). Next or concomitantly, Gram-negative and Gram-positive bacteria induce mechanisms specifically associated with pH resistance such as those involved in the synthesis of degradative amino acid decarboxylases (Auger et al, 1989;Castanie-Cornet et al, 1999;Gale, 1946;Rescei & Snell, 1972;Tabor & Tabor, 1985).…”

Section: Introductionmentioning

confidence: 99%

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

et al. 2004

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In several Gram-positive and Gram-negative bacteria glutamate decarboxylases play an important role in the maintenance of cellular homeostasis in acid environments. Here, new insight is brought to the regulation of the acid response in Escherichia coli. Overexpression of yhiE, similarly to overexpression of gadX, a known regulator of glutamate decarboxylase expression, leads to increased resistance of E. coli strains under high acid conditions, suggesting that YhiE is a regulator of gene expression in the acid response. Target genes of both YhiE (renamed GadE) and GadX were identified by a transcriptomic approach. In vitro experiments with GadE purified protein provided evidence that this regulator binds to the promoter region of these target genes. Several of them are clustered together on the chromosome and this chromosomal organization is conserved in many E. coli strains. Detailed structural (in silico) analysis of this chromosomal region suggests that the promoters of the corresponding genes are preferentially denatured. These results, along with the G+C signature of the chromosomal region, support the existence of a fitness island for acid adaptation on the E. coli chromosome.

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Section: Introductionmentioning

confidence: 99%

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

et al. 2004

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“…The biosynthetic decarboxylases are constitutively expressed regardless of variations in pH and are involved in the synthesis of polyamines (57). The biodegradative decarboxylases, such as arginine and lysine decarboxylases, are strongly induced in rich medium at a low pH in the presence of excess substrate (4,5,21,39,44,52,57) and appear to play a role in pH homeostasis by consuming protons and neutralizing the acidic by-products produced during carbohydrate fermentation (22,49). Biodegradative arginine decarboxylase acts on arginine to produce agmatine and has been thoroughly characterized (5)(6)(7)(8)52).…”

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confidence: 99%

Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli

Stim

Bennett

1993

J Bacteriol

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Arginine decarboxylase (encoded by adi) is induced under conditions of acidic pH, anaerobiosis, and rich medium. The DNA sequence of a 3-kb fragment of the Escherichia coli chromosome encoding biodegradative arginine decarboxylase was determined. This sequence encodes a protein of 755 amino acids with a molecular size of 84,420 daltons. The molecular weight and predicted Adi amino acid composition agree with those found in earlier work. The amino acid sequence of arginine decarboxylase showed homology to those of three other decarboxylases of E. cofi: (i) CadA, encoding lysine decarboxylase; (ii) SpeC, encoding biosynthetic ornithine decarboxylase; and (iii) SpeF, encoding biodegradative ornithine decarboxylase and the lysine decarboxylase of Hafnia alvei. Unlike SpeC and SpeF, Adi is not similar to the biosynthetic arginine decarboxylase, SpeA. adi is also dissimilar to cad4 and speF in that it does not appear to be part of an operon containing a metabolically related transport protein, indicating that it represents a new type of biodegradative decarboxylase regulation. Transcriptional fusions between fragments upstream of adi and lacZ, primer extension, and site-directed mutagenesis experiments defined the pH-regulated promoter. Deletion analysis of the upstream region and cloning of fragments to make adi::lacZ protein fusions implicated a region beyond an upstream SspI site in pH regulation. Induction of adi in the presence of sublethal concentrations of novobiocin or coumermycin Al, inhibitors of DNA gyrase, was dramatically decreased, indicating that DNA supercoiling is involved in adi expression. These results and those of promoter structure studies indicated that acid regulation of adi may involve a mechanism different from that of acid regulation of cad.

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“…30a has similar kinetic properties to its PLP-dependent analog from Morganella morganii (Table II). However, only the activity of the pyruvoyl-dependent enzyme is exquisitely regulated by pH (34,48). Although most proton-consuming decarboxylation reactions are faster at acidic pH, low pH specifically stabilizes an ion pair between Asp 198 of the PvlHisDC ␣-subunit and Asp 53 of an adjacent ␤-subunit to align active site residues (35).…”

Section: Discussionmentioning

confidence: 99%

“…At pH 6.0 and 83°C, the enzyme's turnover number increases to 2.7 s Ϫ1 , with K m ϭ 7.1 Ϯ 1.0 mM and V max ϭ 9.0 Ϯ 0.6 units/mg. The pyruvoyl-dependent histidine decarboxylase enzyme undergoes a pH-dependent conformational change that significantly reduces activity and increases the K m by several orders of magnitude at neutral pH (34,35). However, no comparable change was observed in the PvlArgDC, for which K m ϭ 3.8 Ϯ 0.5 mM and V max nidine and methylguanidine reduced activity by at least 50% at 5-10 mM concentrations.…”

Section: Identification Expression and Purification Of M Jannaschiimentioning

confidence: 99%

Methanococcus jannaschii Uses a Pyruvoyl-dependent Arginine Decarboxylase in Polyamine Biosynthesis

Graham

White

2002

Journal of Biological Chemistry

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The genome sequence of the hyperthermophilic methanogen Methanococcus jannaschii contains homologs of most genes required for spermidine polyamine biosynthesis. Yet genomes from neither this organism nor any other euryarchaeon have orthologs of the pyridoxal 5-phosphate-dependent ornithine or arginine decarboxylase genes, required to produce putrescine. Instead, as shown here, these organisms have a new class of arginine decarboxylase (PvlArgDC) formed by the self-cleavage of a proenzyme into a 5-kDa subunit and a 12-kDa subunit that contains a reactive pyruvoyl group. Although this extremely thermostable enzyme has no significant sequence similarity to previously characterized proteins, conserved active site residues are similar to those of the pyruvoyl-dependent histidine decarboxylase enzyme, and its subunits form a similar (␣␤) 3 complex. Homologs of PvlArgDC are found in several bacterial genomes, including those of Chlamydia spp., which have no agmatine ureohydrolase enzyme to convert agmatine (decarboxylated arginine) into putrescine. In these intracellular pathogens, PvlArgDC may function analogously to pyruvoyl-dependent histidine decarboxylase; the cells are proposed to import arginine and export agmatine, increasing the pH and affecting the host cell's metabolism. Phylogenetic analysis of PvlArgDC proteins suggests that this gene has been recruited from the euryarchaeal polyamine biosynthetic pathway to function as a degradative enzyme in bacteria.

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Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic properties

Cited by 94 publications

References 9 publications

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli

Methanococcus jannaschii Uses a Pyruvoyl-dependent Arginine Decarboxylase in Polyamine Biosynthesis

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