L-Amino Acid Oxidases with Specificity for Basic L-Amino Acids in Cyanobacteria

Gau, Achim E.; Heindl, Achim; Nodop, Anke; Kahmann, Uwe; Pistorius, Elfriede K.

doi:10.1515/znc-2007-3-419

Cited by 14 publications

(26 citation statements)

References 43 publications

(54 reference statements)

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“…; Gau et al. ). On the other hand, arginine:glycine amidinotransferases involved in secondary metabolism have been described in some cyanobacteria (Muenchhoff et al.…”

Section: Introductionmentioning

confidence: 97%

Inactivation of agmatinase expressed in vegetative cells alters arginine catabolism and prevents diazotrophic growth in the heterocyst‐forming cyanobacterium Anabaena

Burnat

Flores

2014

MicrobiologyOpen

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Arginine decarboxylase produces agmatine, and arginase and agmatinase are ureohydrolases that catalyze the production of ornithine and putrescine from arginine and agmatine, respectively, releasing urea. In the genome of the filamentous, heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120, ORF alr2310 putatively encodes an ureohydrolase. Cells of Anabaena supplemented with [14C]arginine took up and catabolized this amino acid generating a set of labeled amino acids that included ornithine, proline, and glutamate. In an alr2310 deletion mutant, an agmatine spot appeared and labeled glutamate increased with respect to the wild type, suggesting that Alr2310 is an agmatinase rather than an arginase. As determined in cell-free extracts, agmatinase activity could be detected in the wild type but not in the mutant. Thus, alr2310 is the Anabaena speB gene encoding agmatinase. The Δalr2310 mutant accumulated large amounts of cyanophycin granule polypeptide, lacked nitrogenase activity, and did not grow diazotrophically. Growth tests in solid media showed that agmatine is inhibitory for Anabaena, especially under diazotrophic conditions, suggesting that growth of the mutant is inhibited by non-metabolized agmatine. Measurements of incorporation of radioactivity from [14C]leucine into macromolecules showed, however, a limited inhibition of protein synthesis in the Δalr2310 mutant. Analysis of an Anabaena strain producing an Alr2310-GFP (green fluorescent protein) fusion showed expression in vegetative cells but much less in heterocysts, implying compartmentalization of the arginine decarboxylation pathway in the diazotrophic filaments of this heterocyst-forming cyanobacterium.

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“…; Gau et al. ). On the other hand, arginine:glycine amidinotransferases involved in secondary metabolism have been described in some cyanobacteria (Muenchhoff et al.…”

Section: Introductionmentioning

confidence: 97%

Inactivation of agmatinase expressed in vegetative cells alters arginine catabolism and prevents diazotrophic growth in the heterocyst‐forming cyanobacterium Anabaena

Burnat

Flores

2014

MicrobiologyOpen

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“…It is known that a number of proteins and enzymes reside on the cell wall and outer membrane of phytoplankton, such as high-affinity binding proteins [7, 8], transporters [9–14], stress proteins [15], signaling proteins [16], and ectoenzymes [17–25]. These proteins play important roles ranging from nutrient utilization, defense, signaling, and cell adhesion to cell-cell recognition.…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of Cell Wall Proteins of a Toxic DinoflagellateAlexandrium catenellaUsing 2-D DIGE and MALDI TOF-TOF Mass Spectrometry

Wang

Dong

et al. 2011

Evidence-Based Complementary and Alternative Medicine

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The cell wall is an important subcellular component of dinoflagellate cells with regard to various aspects of cell surface-associated ecophysiology, but the full range of cell wall proteins (CWPs) and their functions remain to be elucidated. This study identified and characterized CWPs of a toxic dinoflagellate, Alexandrium catenella, using a combination of 2D fluorescence difference gel electrophoresis (DIGE) and MALDI TOF-TOF mass spectrometry approaches. Using sequential extraction and temperature shock methods, sequentially extracted CWPs and protoplast proteins, respectively, were separated from A. catenella. From the comparison between sequentially extracted CWPs labeled with Cy3 and protoplast proteins labeled with Cy5, 120 CWPs were confidently identified in the 2D DIGE gel. These proteins gave positive identification of protein orthologues in the protein database using de novo sequence analysis and homology-based search. The majority of the prominent CWPs identified were hypothetical or putative proteins with unknown function or no annotation, while cell wall modification enzymes, cell wall structural proteins, transporter/binding proteins, and signaling and defense proteins were tentatively identified in agreement with the expected role of the extracellular matrix in cell physiology. This work represents the first attempt to investigate dinoflagellate CWPs and provides a potential tool for future comprehensive characterization of dinoflagellate CWPs and elucidation of their physiological functions.

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“…Synechococcus elongatus L-aao was found in the membrane where it helps in photosynthesis as part of photosystem II particles [5]. Different localization of L-aao was reported in Meleagris gallopavo [6] in mitochondria, while Chlamydomonas reinhardtii [7] and Synechococcus elongatus L-aao were found in the periplasm [8]. Soluble L-aao was also reported from Corynebacterium sp [9] and Neurospora crassa [10].…”

Section: Physiological Role Of L-aaomentioning

confidence: 99%

L-Amino Acid Oxidases-Microbial and Snake Venom

Singh¹

2014

J Microb Biochem Technol

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L-amino acid oxidases (EC 1.4.3.2, are flavoenzymes that catalyse the stereospecific deamination of an L-amino acid to their corresponding α-keto acid with the production of hydrogen peroxide and ammonia. These enzymes are widely distributed across diverse phyla from bacteria, fungi to mammals and many venomous snakes. Although they are mainly involved in cellular amino acid catabolism, many other physiological functions are attributed to L-aao including their antibacterial property and ability to protect from infection. L-aao has also been correlated with penicillin production, violacein synthesis and biofilm development and cell dispersal. Snake venom L-aaos are studied extensively for their ability to induce apoptosis, aggregate platelets, induce haemorrhage, edema and many other toxic effects. L-aaos have been characterized biochemically and found to differ in terms of biochemical parameters not only among different species but also among members of the same species. L-aao act on L-amino acids, preferentially basic, aromatic and aliphatic L-amino acids. The snake venom enzyme shows broad oxidizing activity towards aromatic and hydrophobic L-amino acids such as leucine, phenylalanine and isoleucine.L-aaos have practical value in biochemical and chemical investigations as they have been used to destroy Lisomer of a racemic DL-amino acid and thus yield an optically pure preparation of the D-isomer. As such, L-aao finds numerous applications as catalysts in biotransformation and for production of keto acids. L-aao has also been used for the determination of L-amino acids as part of biosensors. L-amino acids are reported to be found in physiological fluids of patients with certain diseases and disorders. In addition, the content of certain amino acids essentially controls the nutritional quality of the food. L-aao is useful in this aspect by development of biosensors to detect the L-amino acids.Snake venom L-aaos are known to induce apoptosis and antibacterial effects mediated by the hydrogen peroxide produced during the L-aao reaction. The hydrogen peroxide induces oxidative stress which in turn activates the heat shock proteins and initiates an array of functions ultimately leading to apoptosis and cell death. In this aspect, L-aao can be greatly useful for the development of efficient therapeutics and drugs to control tumor cells, bacterial, leishmanicidal, viral and protozoal infections. L-aao is also reported to display dose dependent inhibition on HIV-1 infection and replication and as such can be studied for development of anti HIV medicine.

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L-Amino Acid Oxidases with Specificity for Basic L-Amino Acids in Cyanobacteria

Cited by 14 publications

References 43 publications

Inactivation of agmatinase expressed in vegetative cells alters arginine catabolism and prevents diazotrophic growth in the heterocyst‐forming cyanobacterium Anabaena

Inactivation of agmatinase expressed in vegetative cells alters arginine catabolism and prevents diazotrophic growth in the heterocyst‐forming cyanobacterium Anabaena

Identification and Characterization of Cell Wall Proteins of a Toxic DinoflagellateAlexandrium catenellaUsing 2-D DIGE and MALDI TOF-TOF Mass Spectrometry

L-Amino Acid Oxidases-Microbial and Snake Venom

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