Purification and physical properties of inducible Escherichia coli lysine decarboxylase

Sabo, Donna L.; Boeker, Elizabeth A.; Byers, Breck; Waron, Hannah; Fischer, Edmond H.

doi:10.1021/bi00701a005

Cited by 126 publications

(104 citation statements)

References 34 publications

(15 reference statements)

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“…10 M LdcI (Fig. 6B, panel 2) also elutes as a single species, with an apparent molecular mass of 600 kDa probably representing the decameric species that is known to be formed by LdcI (also see below) (55,56). A mixture of 10 M LdcI with excess RavA (18 M) results in a large shift in the migration of both species indicating a strong interaction (Fig.…”

Section: Rava and Viaa Genes Form An Operon Under The Direct Control Ofmentioning

confidence: 88%

“…The regulation of cadBA transcription is rather complex. The operon is induced by low external pH, by the presence of exogenous lysine, and under anaerobic conditions (55,62). The binding of RavA to LdcI leads us to speculate that RavA might also be involved in the bacterial stress response or that the interaction between the two proteins is regulatory in nature.…”

Section: Rava and Viaa Genes Form An Operon Under The Direct Control Ofmentioning

confidence: 99%

“…These observations explain some presence of dimers in our experimental conditions. It should be noted that, based on a visual analysis of individual side views, Sabo et al (55), proposed the orientation of the dimer to be roughly perpendicular to the plane of the ring. On the contrary, our three-dimensional reconstruction unambiguously demonstrates a pronounced rotation of the monomer inside the dimeric building block of the LdcI double-toroid.…”

Section: Rava⅐viaa Might Play a Role In Metal Insertion-our Analysis Ofmentioning

confidence: 99%

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Formation of a Distinctive Complex between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase

Snider

Gutsche

Lin

et al. 2006

Journal of Biological Chemistry

118

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Section: Rava and Viaa Genes Form An Operon Under The Direct Control Ofmentioning

confidence: 88%

Section: Rava and Viaa Genes Form An Operon Under The Direct Control Ofmentioning

confidence: 99%

Section: Rava⅐viaa Might Play a Role In Metal Insertion-our Analysis Ofmentioning

confidence: 99%

See 1 more Smart Citation

Formation of a Distinctive Complex between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase

Snider

Gutsche

Lin

et al. 2006

Journal of Biological Chemistry

118

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“…Kamio and Terawaki (15) purified PLP-dependent lysine decarboxylase from this bacterium and examined its basic properties. In most bacteria, lysine decarboxylase (LDC) functions mainly as an inducible enzyme that appears only under certain conditions such as low pH (29,30). However, LDC in S. ruminantium was suggested to be produced constitutively, based on the analyses of the enzyme activities in the cells grown under various conditions.…”

Section: Cadaverine Biosynthesis and Its Regulation In S Ruminantiummentioning

confidence: 99%

Molecular Basis for the Maintenance of Envelope Integrity in Selenomonas ruminantium: Cadaverine Biosynthesis and Covalent Modification into the Peptidoglycan Play a Major Role

Kojima

Kamio

2012

J Nutr Sci Vitaminol

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Summary Polyamine is a small organic polycation composed of a hydrocarbon backbone with multiple amino groups which ubiquitously exists in all living organisms from bacteria to higher animals. The critical step of polyamine biosynthesis generally includes the amino acid-decarboxylating reaction to produce the primary diamines, such as a synthesis of putrescine (NH 3 ϩ ·(CH 2 ) 4 ·NH 3 ϩ ) from ornithine, and cadaverine (NH 3 ϩ ·(CH 2 ) 5 ·NH 3 ϩ ) from lysine, which are catalyzed by pyridoxal-5 ′ -phosphate (PLP; vitamin B 6 )-dependent decarboxylases. Synthesized polyamines are implicated in a wide variety of cytoplasmic reactions such as DNA replication and protein synthesis, and are essential for proper growth of the organisms. However, in Selenomonas ruminantium , a strictly anaerobic Gram-negative bacterium dominant in sheep rumen, cadaverine displays its function in a quite distinctive scheme compared to the general bacteria reported. It serves as an essential constituent of the peptidoglycan for the maintenance of envelope integrity through an interaction with the periplasm-exposed SLH domain of Mep45, the outer membrane protein of this bacterium. Furthermore, cytoplasmic biosynthesis of cadaverine occurs totally in a eukaryotic-like manner rather than in a conventional way of bacteria. Lysine/ornithine decarboxylase (LDC/ODC), a PLP-dependent enzyme responsible for cadaverine synthesis in this bacterium, displays significant homology to the eukaryotic ODC but not to the general bacterial LDC nor ODC, and its activity is tightly regulated by antizyme-mediated proteolysis, a regulatory process generally found in eukaryotes. These findings represent the biological diversity of this bacterium beyond the preexisting knowledge related to the polyamine-physiology, cell envelope-architecture, and the regulatory system for the enzyme. In this review we will describe (i) the cadaverine-containing peptidoglycan of S. ruminantium : its chemical structure, biosynthesis, and biological function, and (ii) cellular biosynthesis of cadaverine by LDC/ODC and its antizyme-mediated regulation. In addition, we will briefly refer to (iii) the phylogenetic position and characteristics of S. ruminantium and its unique cadaverine-physiology.

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“…Novel characteristics of S. ruminantium LDC LDC (EC 4.1.1.18), which exists in most bacteria, is involved in the biosynthesis of cadaverine, and is mainly known as an inducible enzyme at low pH conditions or by adding lysine to the medium. 118,119) In contrast, cadaverine in S. ruminantium is synthesized from Llysine and transferred to the peptidoglycan as an essential constituent for normal cell growth. 10,11) From the analyses of the enzyme activities in the cells grown under various conditions, unlike that in other bacteria, S. ruminantium LDC is a constitutive enzyme.…”

Section: )mentioning

confidence: 99%

Molecular Dissection of theSelenomonas ruminantiumCell Envelope and Lysine Decarboxylase Involved in the Biosynthesis of a Polyamine Covalently Linked to the Cell Wall Peptidoglycan Layer

Takatsuka

Kamio

2004

Bioscience, Biotechnology, and Biochemistry

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The wild type of Selenomonas ruminantium subsp. lactilytica, which is a strictly anaerobic, Gram-negative bacterium isolated from sheep rumen, requires one of the normal saturated volatile fatty acids with 3 to 10 carbon atoms for its growth in a glucose medium; however, no such obligate requirement of fatty acid is observed when the cells are grown in a lactate medium. This bacterium is characterized by a unique structure of the cell envelope and a novel lysine decarboxylase and its regulatory protein. In the first part of this article, we will refer to the chemical structure of phospholipid and lipopolysaccharide in the cell membranes of this bacterium compared with that from the general Gramnegative bacteria for understanding their biological functions. S. ruminantium has neither free nor bound forms of Braun lipoprotein which plays an important role of the maintenance of the structural integrity of the cell surface in general Gram-negative bacteria. However, S. ruminantium has cadaverine, which links covalently to the peptidoglycan as a pivotal constituent for the cell division. In the second part of this article, we will refer to the chemical structure of the cadaverinecontaining peptidoglycan, its biosynthesis, and the biological function. In the third part of this article, we will depict the molecular cloning of the genes encoding S. ruminanitum lysine decarboxylase (LDC) and its regulatory protein of 22-kDa (22-kDa protein; P22) which has similar characteristics to that of antizyme of ornithine decarboxylase in eukaryotic cells, and the molecular dissection of these proteins for understanding the regulation of cadaverine biosynthesis. Finally, we will illustrate a proposed structure of the cell envelope, a processes of biosynthesis of the cadaverine-containing peptidoglycan layer, and the LDC degradation mechanism in S. ruminantium, on the basis of the analyses of the cell envelope components, the results from the in vitro experiments on the biosynthesis of the peptidoglycan layer, and the current status of the knowledge on LDC and P22 in this organism.

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Purification and physical properties of inducible Escherichia coli lysine decarboxylase

Cited by 126 publications

References 34 publications

Formation of a Distinctive Complex between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase

Formation of a Distinctive Complex between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase

Molecular Basis for the Maintenance of Envelope Integrity in Selenomonas ruminantium: Cadaverine Biosynthesis and Covalent Modification into the Peptidoglycan Play a Major Role

Molecular Dissection of theSelenomonas ruminantiumCell Envelope and Lysine Decarboxylase Involved in the Biosynthesis of a Polyamine Covalently Linked to the Cell Wall Peptidoglycan Layer

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