The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an l-amino acid oxidase

Gómez, Daniel; Espinosa, Elena; Bertazzo, Marcelo; Lucas-Elı́o, Patricia; Solano, Francisco; Sánchez-Amat, Antonio

doi:10.1007/s00253-008-1499-x

Cited by 46 publications

(43 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…LAAOs can function as toxins in defensive or offensive systems. Examples include the venomous enzymes of snakes in which LAAOs function in prey capture and in defense from predators, [2] secreted enzymes for allelopathy between bacterial species, [3][4][5] enzymatic chemical defenses in marine algae against parasites [6] and in mucus of fish against microbes, [7,8] and enzymatic antimicrobial and antipredator defenses in secretions of land and marine snails. [9][10][11][12][13] One type of marine snail-the sea harehas FAD-containing LAAOs in its ink.…”

mentioning

confidence: 99%

The Chemistry of Escapin: Identification and Quantification of the Components in the Complex Mixture Generated by an L‐Amino Acid Oxidase in the Defensive Secretion of the Sea Snail Aplysia californica

Kamio

Zheng

et al. 2009

Chemistry A European J

View full text Add to dashboard Cite

Escapin is an L-amino acid oxidase in the ink of a marine snail, the sea hare Aplysia californica, which oxidizes L-lysine (1) to produce a mixture of chemicals which is antipredatory and antimicrobial. The goal of our study was to determine the identity and relative abundance of the constituents of this mixture, using molecules generated enzymatically with escapin and also using products of organic syntheses. We examined this mixture under the natural range of pH values for ink-from approximately 5 at full strength to approximately 8 when fully diluted in sea water. The enzymatic reaction likely forms an equilibrium mixture containing the linear form alpha-keto-epsilon-aminocaproic acid (2), the cyclic imine Delta(1)-piperidine-2-carboxylic acid (3), the cyclic enamine Delta(2)-piperidine-2-carboxylic acid (4), possibly the linear enol 6-amino-2-hydroxy-hex-2-enoic acid (7), the alpha-dihydroxy acid 6-amino-2,2-dihydroxy-hexanoic acid (8), and the cyclic aminol 2-hydroxy-piperidine-2-carboxylic acid (9). Using NMR and mass spectroscopy, we show that 3 is the major component of this enzymatic product at any pH, but at more basic conditions, the equilibrium shifts to produce relatively more 4, and at acidic conditions, the equilibrium shifts to produce relatively more 2, 7, and/or 9. Studies of escapin's enzyme kinetics demonstrate that because of the high concentrations of escapin and L-lysine in the ink secretion, millimolar concentrations of 3, H(2)O(2), and ammonia are produced, and also lower concentrations of 2, 4, 7, and 9 as a result. We also show that reactions of this mixture with H(2)O(2) produce delta-aminovaleric acid (5) and delta-valerolactam (6), with 6 being the dominant component under the naturally acidic conditions of ink. Thus, the product of escapin's action on L-lysine contains an equilibrium mixture that is more complex than previously known for any L-amino acid oxidase.

show abstract

mentioning

confidence: 99%

The Chemistry of Escapin: Identification and Quantification of the Components in the Complex Mixture Generated by an L‐Amino Acid Oxidase in the Defensive Secretion of the Sea Snail Aplysia californica

Kamio

Zheng

et al. 2009

Chemistry A European J

View full text Add to dashboard Cite

show abstract

“…The Pseudoalteromonas L-aao has broad substrate specificity, oxidizing several amino acids but it shows some preference for L-glutamine [30].…”

Section: Enzymatic Properties Of L-aaosmentioning

confidence: 99%

“…The L-aao produced from Pseudoalteromonas luteoviolacea is also a broad range L-aao which has antimicrobial activity [30].…”

Section: Physiological Role Of L-aaomentioning

confidence: 99%

L-Amino Acid Oxidases-Microbial and Snake Venom

Singh¹

2014

J Microb Biochem Technol

View full text Add to dashboard Cite

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.

show abstract

“…T he genus Pseudoalteromonas is ubiquitous in the marine environment and can synthesize a range of extracellular compounds (4,8) with antimicrobial activity (3,5), especially the pigmented species (1,6). The marine antagonistic bacterium Pseudoalteromonas flavipulchra JG1, with a golden yellow color, was isolated from water used to rear healthy turbot (Scophthalmus maximus) in Qingdao, China (7).…”

mentioning

confidence: 99%

Genome Sequence of Pseudoalteromonas flavipulchra JG1, a Marine Antagonistic Bacterium with Abundant Antimicrobial Metabolites

Tang

Shi

et al. 2012

J Bacteriol

View full text Add to dashboard Cite

The marine bacterium Pseudoalteromonas flavipulchra JG1 can synthesize various antibacterial metabolites, including protein and small molecules. The draft genome of JG1 is about 5.36 Mb and harbors approximate 4,913 genes, which will provide further insight into the synthesis of antimicrobial agents and antagonistic mechanisms of P. flavipulchra against pathogens.

show abstract

The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an l-amino acid oxidase

Cited by 46 publications

References 30 publications

The Chemistry of Escapin: Identification and Quantification of the Components in the Complex Mixture Generated by an L‐Amino Acid Oxidase in the Defensive Secretion of the Sea Snail Aplysia californica

The Chemistry of Escapin: Identification and Quantification of the Components in the Complex Mixture Generated by an L‐Amino Acid Oxidase in the Defensive Secretion of the Sea Snail Aplysia californica

L-Amino Acid Oxidases-Microbial and Snake Venom

Genome Sequence of Pseudoalteromonas flavipulchra JG1, a Marine Antagonistic Bacterium with Abundant Antimicrobial Metabolites

Contact Info

Product

Resources

About