scholarly journals Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica

2005 ◽  
Vol 208 (18) ◽  
pp. 3609-3622 ◽  
Author(s):  
H. Yang
Keyword(s):  
Amino Acid ◽  
Aplysia Californica ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Sea Hare

Characterization of L-amino acid oxidase and antimicrobial activity of aplysianin A, a sea hare-derived antitumor-antimicrobial protein

2003 ◽  
Vol 69 (6) ◽  
pp. 1240-1246 ◽  
Author(s):  
Mitsuru JIMBO ◽  
Fumie NAKANISHI ◽  
Ryuichi SAKAI ◽  
Koji MURAMOTO ◽  
Hisao KAMIYA
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Antimicrobial Protein ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Sea Hare

scholarly journals Identification of Potent Bactericidal Compounds Produced by Escapin, an l-Amino Acid Oxidase in the Ink of the Sea Hare Aplysia californica

2008 ◽  
Vol 52 (12) ◽  
pp. 4455-4462 ◽  
Author(s):  
Ko-Chun Ko ◽  
Binghe Wang ◽  
Phang C. Tai ◽  
Charles D. Derby
Keyword(s):  
Amino Acid ◽  
Bactericidal Activity ◽  
Aplysia Californica ◽  
Aminocaproic Acid ◽  
Equilibrium Mixture ◽  
Bactericidal Effect ◽  
Low Ph ◽  
Acid Oxidase ◽  
Reaction Products ◽  
Amino Acid Oxidase

ABSTRACT The ink of sea hares (Aplysia californica) contains escapin, an l-amino acid oxidase that metabolizes l-lysine, thereby producing a mixture that kills microbes and deters attacking predators. This secretion contains H2O2, ammonia, and an equilibrium mixture of “escapin intermediate product” (EIP-K) that includes α-keto-ε-aminocaproic acid and several other molecules. Components of the equilibrium mixture react nonenzymatically with H2O2 to form “escapin end product” (EEP-K), which contains δ-aminovaleric acid and δ-valerolactam. The proportions of the molecules in this equilibrium mixture change with pH, and this is biologically important because the secretion is pH 5 when released but becomes pH 8 when fully diluted in seawater. The goal of the current study was to identify which molecules in this equilibrium mixture are bactericidal. We show that a mixture of H2O2 and EIP-K, but not EEP-K, at low mM concentrations is synergistically responsible for most of the bactericidal activity of the secretion against Escherichia coli, Vibrio harveyi, Staphylococcus aureus, and Pseudomonas aeruginosa. Low pH enhances the bactericidal effect, and this does not result from stress associated with low pH itself. Sequential exposure to low mM concentrations of EIP-K and H2O2, in either order, does not kill E. coli. Reaction products formed when l-arginine is substituted for l-lysine have almost no bactericidal activity. Our results favor the idea that the bactericidal activity is due to unstable intermediates of the reaction of α-keto-ε-aminocaproic acid with H2O2.

Purification and Characterization of Lupus Anticoagulant Like Protein from Agkistrodon Halys Brevicaudus Venom

1996 ◽  
Vol 76 (06) ◽  
pp. 0993-0997
Author(s):  
Zhao-Yan Li ◽  
Xiao-Wei Wu ◽  
Tie-Fu Yu ◽  
Eric C-Y Lian
Keyword(s):  
Amino Acid ◽  
Lupus Anticoagulant ◽  
Inhibitory Effect ◽  
Clotting Factor ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Sds Page ◽  
The Individual ◽  
Reducing Condition

SummaryBy means of CM-Sephadex C-25, DEAE-Sephadex A-50, Sephadex G-200, and Sephadex G-75 chromatographies, a lupus anticoagulant like protein (LALP) from Agkistrodon halys brevicaudus was purified. On SDS-PAGE, the purified LALP had a molecular weight of 25,500 daltons under non-reducing condition and 15,000 daltons under reducing condition. The isoelectric point was pH 5.6. Its N terminal amino acid sequencing revealed a mixture of 2 sequences: DCP(P/S)(D/G)WSSYEGH(C/R)Q(Q/K). It was devoid of phospho-lipaseA, fibrino(geno)lytic, 5′-nucleotidase, L-amino acid oxidase, phosphomonoesterase, phosphodiesterase and thrombin-like activities, which were found in crude venom. In the presence of LALP, PT, aPTT, and dRVVT of human plasma were markedly prolonged and its effects were concentration-dependent but time-independent. The inhibitory effect of LALP on the plasma clotting time was enhanced by decreasing phospholipid concentration in TTI test. The individual clotting factor activity was not affected by LALP when higher dilutions of LALP-plasma mixture were used for assay. Russell’s viper venom time was shortened when high phospholipid confirmatory reagent was used. Therefore, the protein has lupus anticoagulant property.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

scholarly journals Spinal mechanisms contributing to the development of pain hypersensitivity induced by sphingolipids in the rat

2021 ◽  
Author(s):  
Hong Wei ◽  
Zuyue Chen ◽  
Ari Koivisto ◽  
Antti Pertovaara
Keyword(s):  
Amino Acid ◽  
Nmda Receptors ◽  
Receptor Antagonist ◽  
Gap Junction ◽  
Male Rats ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Mk 801 ◽  
Mechanical Hypersensitivity ◽  
Pain Hypersensitivity

Abstract Background Earlier studies show that endogenous sphingolipids can induce pain hypersensitivity, activation of spinal astrocytes, release of proinflammatory cytokines and activation of TRPM3 channel. Here we studied whether the development of pain hypersensitivity induced by sphingolipids in the spinal cord can be prevented by pharmacological inhibition of potential downstream mechanisms that we hypothesized to include TRPM3, σ1 and NMDA receptors, gap junctions and D-amino acid oxidase. Methods Experiments were performed in adult male rats with a chronic intrathecal catheter for spinal drug administrations. Mechanical nociception was assessed with monofilaments and heat nociception with radiant heat. N,N-dimethylsphingosine (DMS) was administered to induce pain hypersensitivity. Ononetin, isosakuranetin, naringenin (TRPM3 antagonists), BD-1047 (σ1 receptor antagonist), carbenoxolone (a gap junction decoupler), MK-801 (NMDA receptor antagonist) and AS-057278 (inhibitor of D-amino acid oxidase, DAAO) were used to prevent the DMS-induced hypersensitivity, and pregnenolone sulphate (TRPM3 agonist) to recapitulate hypersensitivity. Results DMS alone produced within 15 min a dose-related mechanical hypersensitivity that lasted at least 24 h, without effect on heat nociception. Preemptive treatments with ononetin, isosakuranetin, naringenin, BD-1047, carbenoxolone, MK-801 or AS-057278 attenuated the development of the DMS-induced hypersensitivity, but had no effects when administered alone. Pregnenolone sulphate (TRPM3 agonist) alone induced a dose-related mechanical hypersensitivity that was prevented by ononetin, isosakuranetin and naringenin. Conclusions Among spinal pronociceptive mechanisms activated by DMS are TRPM3, gap junction coupling, the σ1 and NMDA receptors, and DAAO.

scholarly journals Picosecond laser fluorometry of FAD of D-amino acid oxidase-benzoate complex.

1983 ◽  
Vol 258 (6) ◽  
pp. 3799-3802
Author(s):  
K Yagi ◽  
F Tanaka ◽  
N Nakashima ◽  
K Yoshihara
Keyword(s):  
Amino Acid ◽  
Picosecond Laser ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Studies on the Elimination Reaction of d-Amino Acid Oxidase with α-Amino-β-chlorobutyrate

1973 ◽  
Vol 248 (6) ◽  
pp. 1946-1955 ◽  
Author(s):  
Christopher T. Walsh ◽  
Elizabeth Krodel ◽  
Vincent Massey ◽  
Robert H. Abeles
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Elimination Reaction ◽  
Amino Acid Oxidase
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