Evaluation ofD-amino acid oxidase fromRhodotorula gracilisfor the production of α-keto acids: A reactor system

1994 ◽  
Vol 44 (11) ◽  
pp. 1288-1294 ◽  
Author(s):  
Simona Butò ◽  
Loredano Pollegioni ◽  
Luigi D'Angiuro ◽  
Mirella S. Pilone
Keyword(s):  
Amino Acid ◽  
Reactor System ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Keto Acids

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.

Inhibition ofd-amino acid oxidase by α-keto acids analogs of amino acids

1996 ◽  
Vol 18 (5) ◽  
pp. 379-382 ◽  
Author(s):  
JoséA. Moreno ◽  
Francisco J. Montes ◽  
Jacinto Catalán ◽  
Miguel A. Galán
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Keto Acids

THE METABOLISM OF ASCARIS LUMBRICOIDES OVARIES: II. AMINO ACID METABOLISM

1955 ◽  
Vol 33 (1) ◽  
pp. 307-316 ◽  
Author(s):  
John K. Pollak ◽  
Donald Fairbairn
Keyword(s):  
Amino Acid ◽  
Reductive Amination ◽  
Acid Oxidase ◽  
Active Protein ◽  
Amino Acid Oxidase ◽  
Keto Acids ◽  
Glutamic Dehydrogenase ◽  
A Minor ◽  
Pyruvic Acids ◽  
Minor Reaction

Homogenates of ascaris ovaries contained transamination, deamination, and reductive amination systems. Alanine–glutamic and aspartic–glutamic transaminases were active, whereas weaker transaminations occurred between glycine or serine and α-ketoglutaric or pyruvic acids. Sixteen other amino acids did not participate in transamination with these keto acids. A minor reaction, however, occurred between alanine or glutamic acid and α-ketovaleric acid. No amino acid oxidase activity was detected, and deamination appeared to be limited to a weakly positive glutamic dehydrogenase, which could be coupled to the alanine–glutamic and aspartic–glutamic transaminases to form a transdeaminase system. In the presence of pyruvate and ammonium chloride reductive amination occurred and alanine and aspartic acid were synthesized. This reaction was accelerated by bicarbonate, although oxalacetate could not be substituted successfully for pyruvate in the amination system. The results of the investigation are in accord with the probability that an active protein synthesis occurs in ascaris ovaries.

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 Efficient production of α-keto acids by immobilized E. coli -pETduet-1- Pmi LAAO in a jacketed packed-bed reactor

2019 ◽  
Vol 6 (4) ◽  
pp. 182035 ◽  
Author(s):  
Licheng Wu ◽  
Xiaolei Guo ◽  
Gaobing Wu ◽  
Pengfu Liu ◽  
Ziduo Liu
Keyword(s):  
Amino Acid ◽  
Continuous Production ◽  
Packed Bed ◽  
Alginate Beads ◽  
Packed Bed Reactor ◽  
Efficient Production ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
E Coli ◽  
Keto Acids

α-keto acids are compounds of primary interest for the fine chemical, pharmaceutical and agrochemical sectors. l -amino acid oxidases as an efficient tool are used for α-keto acids preparation in this study. Firstly, an l -amino acid oxidase ( Pmi LAAO) from Proteus mirabilis was discovered by data mining . Secondly, by gene expression vector screening, pETDuet-1- Pmi LAAO activity improved by 130%, as compared to the pET20b- Pmi LAAO. Pmi LAAO production was increased to 9.8 U ml −1 by optimized expression condition (OD 600 = 0.65, 0.45 mmol l −1 IPTG, 20 h of induction). Furthermore, The Pmi LAAO was stabile in the pH range of 4.0–9.0 and in the temperature range of 10–40°C; the optimal pH and temperature of recombinant Pmi LAAO were 6.5 and 37°C, respectively. Afterwards, in order to simplify product separation process, E. coli -pETduet-1- Pmi LAAO was immobilized in Ca-alginate beads. Continuous production of 2-oxo-3-phenylpropanoic acid was conducted in a packed-bed reactor via immobilized E. coli -pETduet-1- Pmi LAAO. Significantly, 29.66 g l −1 2-oxo-3-phenylpropanoic acid with a substrate conversion rate of 99.5% was achieved by correspondingly increasing the residence time (25 h). This method holds the potential to be used for efficiently producing pure α-keto acids.

THE METABOLISM OF ASCARIS LUMBRICOIDES OVARIES: II. AMINO ACID METABOLISM

1955 ◽  
Vol 33 (3) ◽  
pp. 307-316 ◽  
Author(s):  
John K. Pollak ◽  
Donald Fairbairn
Keyword(s):  
Amino Acid ◽  
Reductive Amination ◽  
Acid Oxidase ◽  
Active Protein ◽  
Amino Acid Oxidase ◽  
Keto Acids ◽  
Glutamic Dehydrogenase ◽  
A Minor ◽  
Pyruvic Acids ◽  
Minor Reaction

Homogenates of ascaris ovaries contained transamination, deamination, and reductive amination systems. Alanine–glutamic and aspartic–glutamic transaminases were active, whereas weaker transaminations occurred between glycine or serine and α-ketoglutaric or pyruvic acids. Sixteen other amino acids did not participate in transamination with these keto acids. A minor reaction, however, occurred between alanine or glutamic acid and α-ketovaleric acid. No amino acid oxidase activity was detected, and deamination appeared to be limited to a weakly positive glutamic dehydrogenase, which could be coupled to the alanine–glutamic and aspartic–glutamic transaminases to form a transdeaminase system. In the presence of pyruvate and ammonium chloride reductive amination occurred and alanine and aspartic acid were synthesized. This reaction was accelerated by bicarbonate, although oxalacetate could not be substituted successfully for pyruvate in the amination system. The results of the investigation are in accord with the probability that an active protein synthesis occurs in ascaris ovaries.

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