D-amino acid oxidase fromTrigonopsis variabilis: Comparison of enzyme specificity ?in vivo? and ?in vitro?

1985 ◽  
Vol 7 (1) ◽  
pp. 9-14 ◽  
Author(s):  
Eva M. Kubicek-Pranz ◽  
Max R�hr
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Enzyme Specificity ◽  
Amino Acid Oxidase

scholarly journals Protective Role of d-Amino Acid Oxidase against Staphylococcus aureus Infection

2012 ◽  
Vol 80 (4) ◽  
pp. 1546-1553 ◽  
Author(s):  
Hideaki Nakamura ◽  
Jun Fang ◽  
Hiroshi Maeda
Keyword(s):  
Hydrogen Peroxide ◽  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Bactericidal Activity ◽  
Hypochlorous Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Content Type

ABSTRACTd-Amino acid oxidase (DAO) is a hydrogen peroxide-generating enzyme that uses ad-amino acid as a substrate. We hypothesized that DAO may protect against bacterial infection, because hydrogen peroxide is one of the most important molecules in the antibacterial defense systems in mammals. We show here that DAO suppressed the growth ofStaphylococcus aureusin a manner that depended on the concentration of DAO andd-amino acidin vitro. Addition of catalase abolished the bacteriostatic activity of DAO. Although DAO plusd-Ala showed less bactericidal activity, addition of myeloperoxidase (MPO) greatly enhanced the bactericidal activity of DAO. Furthermore, DAO was able to utilize bacterial lysate, which containsd-Ala derived from peptidoglycan; this could produce hydrogen peroxide with, in the presence of myeloperoxidase, formation of hypochlorous acid. This concerted reaction of DAO and MPO led to the bactericidal action.In vivoexperiments showed that DAO−/−(mutant) mice were more susceptible toS. aureusinfection than were DAO+/+(wild-type) mice. These results suggest that DAO, together with myeloperoxidase, may play an important role in antibacterial systems in mammals.

In vivo and in vitro expression of porcine D-amino acid oxidase: in vitro system for the synthesis of a functional enzyme

Biochemistry ◽  
1988 ◽  
Vol 27 (18) ◽  
pp. 6693-6697 ◽  
Author(s):  
Kiyoshi Fukui ◽  
Kyoko Momoi ◽  
Fusao Watanabe ◽  
Yoshihiro Miyake
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
In Vitro System ◽  
In Vitro Expression

In vitro and in vivo pharmacological profile of AS057278, a selective d-amino acid oxidase inhibitor with potential anti-psychotic properties

2008 ◽  
Vol 18 (3) ◽  
pp. 200-214 ◽  
Author(s):  
Tiziana Adage ◽  
Anne-Cécile Trillat ◽  
Anna Quattropani ◽  
Dominique Perrin ◽  
Laurent Cavarec ◽  
...  
Keyword(s):  
Amino Acid ◽  
Oxidase Inhibitor ◽  
Acid Oxidase ◽  
Anti Psychotic ◽  
Pharmacological Profile ◽  
Amino Acid Oxidase

scholarly journals The anti-ovarian carcinoma activity of L-amino Acid Oxidase from Crotalus adamanteus venom in vivo and in vitro

2021 ◽  
Author(s):  
Li Bo ◽  
Yan Xiong ◽  
Qiyi He ◽  
Xiaodong Yu ◽  
Bo Li ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Amino Acid ◽  
Cancer Cells ◽  
Morphological Changes ◽  
Complex Mixture ◽  
Ovarian Cancer Cells ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Apoptosis Pathway

Abstract The anti-tumor potential of animal toxins has fully attracted the attention of researchers. Snake venoms is a complex mixture of different components and has revealed high toxicity on normal and tumoral tissues or cells. The snake venom L-Amino-acid oxidase (svLAAO) has grown up to be a critical research target in molecular biology sciences and medicine sciences since widespread presence and various biological roles, including antitumor application. We found that Crotalus adamanteus (C. adamanteus) venom LAAO significantly decreased the viability of ovarian cancer cells and caused morphological changes preceded cell death. Cell experiments confirmed that C. adamanteus venom LAAO caused alterations of intrinsic or extrinsic apoptosis pathway-related genes in ovarian cancer cells. Animal experiments and histological analysis also proved that C. adamanteus venom LAAO could effectively inhibit the damage of ovarian cancer to tissues. The major apoptosis induction of C. adamanteus venom LAAO on ovarian cancer cells can be blocked by catalase, suggesting that the cytotoxicity of C. adamanteus venom LAAO on ovarian cancer cells was mainly mediated by H2O2. Our preliminary results revealed that C. adamanteus venom LAAO may induce apoptosis of ovarian cancer cells through the death receptor pathway and mitochondrial pathway. It is inferred that C. adamanteus venom LAAO will be some advantages in New Drug Research and Development of antitumor drugs in the future. Nevertheless, extra studies on the pharmacological actions and molecular mechanism of svLAAO in anti-cancer are necessary in order to better promote its application.

scholarly journals Effects of D‐amino acid oxidase inhibition on memory performance and long‐term potentiation in vivo

2013 ◽  
Vol 1 (1) ◽  
Author(s):  
Seth C. Hopkins ◽  
Una C. Campbell ◽  
Michele L. R. Heffernan ◽  
Kerry L. Spear ◽  
Ross D. Jeggo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Memory Performance ◽  
Long Term Potentiation ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Term Potentiation ◽  
Oxidase Inhibition

In vitro cytotoxicity of L-amino acid oxidase from the venom of Crotalus mitchellii pyrrhus

Toxicon ◽  
2017 ◽  
Vol 139 ◽  
pp. 20-30 ◽  
Author(s):  
Kok Keong Tan ◽  
Siok Ghee Ler ◽  
Jayantha Gunaratne ◽  
Boon Huat Bay ◽  
Gopalakrishnakone Ponnampalam
Keyword(s):  
Amino Acid ◽  
In Vitro Cytotoxicity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Crotalus Mitchellii

scholarly journals Vipera berus berus Venom from Russia: Venomics, Bioactivities and Preclinical Assessment of Microgen Antivenom

Toxins ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 90 ◽  
Author(s):  
Ruslan I. Al-Shekhadat ◽  
Ksenia S. Lopushanskaya ◽  
Álvaro Segura ◽  
José María Gutiérrez ◽  
Juan J. Calvete ◽  
...  
Keyword(s):  
Binding Capacity ◽  
Secretory Protein ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Vipera Berus ◽  
Phospholipases A2 ◽  
Toxin Binding ◽  
Main Effects

The common European adder, Vipera berus berus, is a medically relevant species, which is widely distributed in Russia and thus, is responsible for most snakebite accidents in Russia. We have investigated the toxic and enzymatic activities and have determined the proteomic composition of its venom. Phospholipases A2 (PLA2, 25.3% of the venom proteome), serine proteinases (SVSP, 16.2%), metalloproteinases (SVMP, 17.2%), vasoactive peptides (bradykinin-potentiating peptides (BPPs), 9.5% and C-type natriuretic peptides (C-NAP, 7.8%), cysteine-rich secretory protein (CRISP, 8%) and L-amino acid oxidase (LAO, 7.3%) represent the major toxin classes found in V. b. berus (Russia) venom. This study was also designed to assess the in vivo and in vitro preclinical efficacy of the Russian Microgen antivenom in neutralizing the main effects of V. b. berus venom. The results show that this antivenom is capable of neutralizing the lethal, hemorrhagic and PLA2 activities. Third-generation antivenomics was applied to quantify the toxin-recognition landscape and the maximal binding capacity of the antivenom for each component of the venom. The antivenomics analysis revealed that 6.24% of the anti-V. b. berus F(ab’)2 molecules fraction are toxin-binding antibodies, 60% of which represent clinically relevant antivenom molecules.

Role of renal d-amino-acid oxidase in pharmacokinetics of d-leucine

2004 ◽  
Vol 287 (1) ◽  
pp. E160-E165 ◽  
Author(s):  
Hiroshi Hasegawa ◽  
Takehisa Matsukawa ◽  
Yoshihiko Shinohara ◽  
Ryuichi Konno ◽  
Takao Hashimoto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Renal Mass ◽  
Acid Oxidase ◽  
Mass Reduction ◽  
Chiral Inversion ◽  
Amino Acid Oxidase ◽  
Isotope Tracer ◽  
Keto Acids

d-Amino acids are now recognized to be widely present in mammals. Renal d-amino-acid oxidase (DAO) is associated with conversion of d-amino acids to the corresponding α-keto acids, but its contribution in vivo is poorly understood because the α-keto acids and/or l-amino acids formed are indistinguishable from endogenous compounds. First, we examined whether DAO is indispensable for conversion of d-amino acids to their α-keto acids by using the stable isotope tracer technique. After a bolus intravenous administration of d-[2H7]leucine to mutant mice lacking DAO activity (ddY/DAO−) and normal mice (ddY/DAO+), elimination of d-[2H7]leucine and formation of α-[2H7]ketoisocaproic acid ([2H7]KIC) and l-[2H7]leucine in plasma were determined. The ddY/DAO− mice, in contrast to ddY/DAO+ mice, failed to convert d-[2H7]leucine to [2H7]KIC and l-[2H7]leucine. This result clearly revealed that DAO was indispensable for the process of chiral inversion of d-leucine. We further investigated the effect of renal mass reduction by partial nephrectomy on elimination of d-[2H7]leucine and formation of [2H7]KIC and l-[2H7]leucine. Renal mass reduction slowed down the elimination of d-[2H7]leucine. The fraction of conversion of d-[2H7]leucine to [2H7]KIC in sham-operated rats was 0.77, whereas that in five-sixths-nephrectomized rats was 0.25. The elimination behavior of d-[2H7]leucine observed in rats suggested that kidney was the principal organ responsible for converting d-leucine to KIC.

scholarly journals Evaluation of human D-amino acid oxidase inhibition by anti-psychotic drugs in vitro

2014 ◽  
Vol 8 (3) ◽  
pp. 149-154 ◽  
Author(s):  
Miho Shishikura ◽  
Hitomi Hakariya ◽  
Sumiko Iwasa ◽  
Takashi Yoshio ◽  
Hideaki Ichiba ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Anti Psychotic ◽  
Amino Acid Oxidase ◽  
Oxidase Inhibition
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