scholarly journals CONSTITUENTS OF ELEMENTARY BODIES OF VACCINIA

1941 ◽  
Vol 74 (2) ◽  
pp. 133-144 ◽  
Author(s):  
Charles L. Hoagland ◽  
S. M. Ward ◽  
Joseph E. Smadel ◽  
Thomas M. Rivers
Keyword(s):  
Amino Acid ◽  
Ultraviolet Light ◽  
Flavin Adenine Dinucleotide ◽  
Specific Protein ◽  
Microbiological Assay ◽  
Acid Oxidase ◽  
Animal Cells ◽  
Oxidative Deamination ◽  
Amino Acid Oxidase ◽  
Chromatographic Methods

Suspensions of purified elementary bodies of vaccinia exhibit fluorescence in the presence of ultraviolet light. This fluorescent constituent can be separated by chromatographic methods provided the virus is first denatured by acid and heat. By means of the specific protein of d-amino acid oxidase it has been possible to identify the flavin constituent as flavin-adenine-dinucleotide and show that it can participate in the oxidative deamination of d-alanine. By means of microbiological assay the flavin component has been quantitatively measured and shown to compare favorably in concentration with that observed in animal cells and in some bacteria; its concentration in virus is lower than that observed in yeast. The demonstration that it exists as an integral portion of the virus is not conclusive. So far, however, it has been separated from the elementary bodies only by means which in themselves inactivate the virus.

scholarly journals TINJAUAN, D-ASAM AMINO OKSIDASE DARI MIKROBA: PRODUKSI DAN APLIKASI

2015 ◽  
Vol 2 (2) ◽  
pp. 88
Author(s):  
Ahmad Wibisana ◽  
Indria Puti Mustika
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Carbon Source ◽  
Flavin Adenine Dinucleotide ◽  
Acid Oxidase ◽  
Amino Acid Production ◽  
Oxidative Deamination ◽  
Amino Acid Oxidase ◽  
Keto Acids ◽  
Biotechnology Application

D-amino acid oxidase (DAAO) is a flavin adenine dinucleotide-containing enzyme that catalyzes the oxidative deamination of amino acid D-isomers with high stereospecificity, which results in α-keto acids, ammonia and hydrogen peroxide. Having high stereospecificity, DAAO is used in a variety of applications such as drug, biocatalyst, biosensor and preparation of transgenic plants. DAAO is widespread in nature, found in microorganisms to mammals. Microbial DAAO is considered more important than mammalian DAAO for biotechnology application. DAAO production in submerged fermentation is influenced by several factors, such as carbon source, nitrogen source, inducer, dissolve oxygen, temperature and pH. The influence of those factors on DAAO production by microbial origin, DAAO production by microbial recombinant, and its application in biotechnology are discussed in this review.Keywords: Enzyme, DAAO, D-amino acid, production, application ABSTRAKEnzim D-asam amino oksidase (DAAO) merupakan enzim yang mengandung Flavin Adenine Dinucleotide yang bekerja mengkatalisis reaksi oksidasi deaminasi D-asam amino dengan stereospesifisitas yang tinggi menghasilkan α-asam keto, amonia dan hidrogen peroksida. Karena mempunyai karakteristik sreteospesifisitas yang tinggi, enzim DAAO banyak digunakan untuk berbagai aplikasi seperti obat, biokatalis, biosensor dan penyiapan tanaman transgenik. Enzim ini dapat dihasilkan oleh organisme mulai dari bakteri hingga mamalia, namun untuk aplikasi dibidang bioteknologi, enzim DAAO yang berasal dari mikroorganisme dipandang lebih penting dari pada yang berasal dari mamalia. Produksi enzim dari DAAO dari mikroorganisme dalam kultur cair dipengaruhi oleh beberapa faktor seperti sumber karbon, nitrogen, senyawa penginduksi, oksigen terlarut, temperatur dan pH medium. Pengaruh dari faktor-faktor tersebut terhadap produksi enzim DAAO, produksi enzim DAAO menggunakan mikroba rekombinan serta aplikasinya dalam bidang bioteknologi dibahas dalam tinjauan.Kata Kunci: Enzim, DAAO, D-asam amino, produksi, aplikasi

scholarly journals The Pseudoalteromonas luteoviolacea L-amino Acid Oxidase with Antimicrobial Activity Is a Flavoenzyme

Marine Drugs ◽  
2018 ◽  
Vol 16 (12) ◽  
pp. 499 ◽  
Author(s):  
Andrés Andreo-Vidal ◽  
Antonio Sanchez-Amat ◽  
Jonatan Campillo-Brocal
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Flavin Adenine Dinucleotide ◽  
Sequence Similarity ◽  
Bacterial Species ◽  
Biological Significance ◽  
Acid Oxidase ◽  
Biotechnological Applications ◽  
Amino Acid Oxidase ◽  
First Time

The marine environment is a rich source of antimicrobial compounds with promising pharmaceutical and biotechnological applications. The Pseudoalteromonas genus harbors one of the highest proportions of bacterial species producing antimicrobial molecules. For decades, the presence of proteins with L-amino acid oxidase (LAAO) and antimicrobial activity in Pseudoalteromonas luteoviolacea has been known. Here, we present for the first time the identification, cloning, characterization and phylogenetic analysis of Pl-LAAO, the enzyme responsible for both LAAO and antimicrobial activity in P. luteoviolacea strain CPMOR-2. Pl-LAAO is a flavoprotein of a broad substrate range, in which the hydrogen peroxide generated in the LAAO reaction is responsible for the antimicrobial activity. So far, no protein with a sequence similarity to Pl-LAAO has been cloned or characterized, with this being the first report on a flavin adenine dinucleotide (FAD)-containing LAAO with antimicrobial activity from a marine microorganism. Our results revealed that 20.4% of the sequenced Pseudoalteromonas strains (specifically, 66.6% of P. luteoviolacea strains) contain Pl-laao similar genes, which constitutes a well-defined phylogenetic group. In summary, this work provides insights into the biological significance of antimicrobial LAAOs in the Pseudoalteromonas genus and shows an effective approach for the detection of novel LAAOs, whose study may be useful for biotechnological applications.

Sign in / Sign up

Export Citation Format

Share Document