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1.
Chinese Journal of Contemporary Pediatrics ; (12): 416-419, 2021.
Article in Chinese | WPRIM | ID: wpr-879869

ABSTRACT

A boy attended the hospital at the age of 1 month due to left hand tremor for 1 week. A blood test showed a reduction in serum uric acid and a cranial MRI showed encephalomalacia, atrophy, and cystic changes. The boy had microcephalus, unusual facial features (long face, long forehead, protruded forehead, long philtrum, low nasal bridge, facial swelling, and thick lower lip), hypertonia of lower extremities, and severe global developmental delay. Whole-exome sequencing performed for the boy detected a homozygous mutation, c.217C > T(p.R73W), in the


Subject(s)
Humans , Infant, Newborn , Male , Carbon-Carbon Lyases , China , Metal Metabolism, Inborn Errors , Mutation , Uric Acid
2.
Braz. j. microbiol ; 46(1): 97-102, 05/2015. tab
Article in English | LILACS | ID: lil-748258

ABSTRACT

Salinity is the leading abiotic stress hampering maize (Zea mays L.) growth throughout the world, especially in Pakistan. During salinity stress, the endogenous ethylene level in plants increases, which retards proper root growth and consequent shoot growth of the plants. However, certain bacteria contain the enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase, which converts 1-aminocyclopropane-1-carboxylic acid (an immediate precursor of ethylene biosynthesis in higher plants) into ammonia and α-ketobutyrate instead of ethylene. In the present study, two Pseudomonas bacterial strains containing ACC-deaminase were tested separately and in combinations with mineral fertilizers to determine their potential to minimize/undo the effects of salinity on maize plants grown under saline-sodic field conditions. The data recorded at 30, 50 and 70 days after sowing revealed that both the Pseudomonas bacterial strains improved root and shoot length, root and shoot fresh weight, and root and shoot dry weight up to 34, 43, 35, 71, 55 and 68%, respectively, when applied without chemical fertilizers: these parameter were enhanced up to 108, 95, 100, 131, 100 and 198%, respectively, when the strains were applied along with chemical fertilizers. It can be concluded that ACC-deaminase Pseudomonas bacterial strains applied alone and in conjunction with mineral fertilizers improved the root and shoot growth of maize seedlings grown in saline-sodic soil.


Subject(s)
Plant Development , Plant Roots/physiology , Plant Shoots/physiology , Pseudomonas/growth & development , Soil Microbiology , Soil/chemistry , Zea mays/physiology , Amino Acids, Cyclic/metabolism , Ammonia/metabolism , Butyrates , Carbon-Carbon Lyases/metabolism , Fertilizers , Pakistan , Pseudomonas/enzymology , Salinity
3.
IJB-Iranian Journal of Biotechnology. 2014; 12 (3): 50-56
in English | IMEMR | ID: emr-167786

ABSTRACT

Many plant growth-promoting bacteria including Rhizobia contain the 1-aminocyclopropane-1-carboxylate [ACC] deaminase enzyme that can leave ACC, and thereby lower the level of ethylene in stressed plants. Drought and salinity are the most common environmental stress factors for plants in Iran. The main aim of this research was development of bio-fertilizers containing ACC deaminase enzyme which is very important in conditions of stressed drought and salinity. In this research 168 isolates of native Sinorhizobium meliloti were evaluated for ACC deaminase activity. These isolates were classified in four groups based on growth rate on ACC containing medium and enzyme activity. One isolate from each group was selected for molecular characterization. The nucleotide sequence of 16S rRNA gene of the selected isolates were determined. The ACC deaminase genes [acdS] on total and chromosomal DNA of S. meliloti KYA40, and KYA71 strains were isolated and cloned in pTZ57R/T vector and the obtained recombinant plasmids were used for sequence analysis. The sequence of acdS genes from strains KYA71 and KYA40 and corresponding proteins were analyzed with respect to available sequences in NCBI database. The 16S rRNA gene sequences of S. meliloti strains submitted to the GeneBank/NCBI database. The acdS gene of KYA71 may be located on chromosomal DNA and in KYA40 it is located on one of the mega plasmids. These two genes have 99% similarity with three nucleotide differences which only lead to a change in one amino acid 48, threonine in KYA40 acdS gene and methionine in KYA71. The comparison of amino acid sequences of KYA40 and KYA71 with other sequences in the database showed that the amino acids 37 to 58 in almost all strains were similar. Therefore, it was concluded that it was a conserved region in this location of acdS genes and any changes in this region may cause change in ACC deaminase activity


Subject(s)
Carbon-Carbon Lyases/genetics , Sequence Analysis , Cloning, Molecular
4.
Acta sci., Biol. sci ; 34(4): 419-428, Oct.-Dec. 2012. graf, tab
Article in English | LILACS, VETINDEX | ID: biblio-859675

ABSTRACT

The aim of this study is to evaluate the kinetics of aerobic decomposition of Saccharum officinarum and Talauma ovata leaves. For each species, decomposition chambers (leaves and water) were set up, which were maintained under controlled conditions. Each sampling day (1, 7, 15, 30, 39, 58, 72 and 90 days), the concentrations of total organic carbon, pH and electrical conductivity (EC) were determined in the dissolved fraction, while the mass and cell wall fractions (CWF) were determined in the particulate fraction. The pH stabilization of the chambers with T. ovata and S. officinarum leaves occurred in alkaline (ca. 8 - 8.5) and close to the neutrality (ca. 7 - 7.5) environment, respectively. The EC values were on average 1.6 times higher in incubations with T. ovata leaves. The mass loss did not differ between the species (mean = 53.85%), however the decay coefficient was higher for S. officinarum (k4 = 0.007 day-1) than for T. ovata (k4 = 0.005 day-1) leaves. The CWF mass loss (mean = 50.16%) and their coefficient (0.0090 day-1) were similar. S. officinarum decomposed faster due to its high concentrations of energetic compounds of interest to the microbiota. The slower decomposition of T. ovata may have occurred due to the presence of secondary compounds with negative effects to the microorganisms.


O objetivo deste estudo foi avaliar as cinéticas da decomposição aeróbia de folhas de Talauma ovata e Saccharum officinarum. Para cada espécie foram montadas câmaras de decomposição (folhas e água) que foram mantidas sob condições controladas. A cada dia amostral (1, 7, 15, 30, 39, 58, 72 e 90 dias), as concentrações de carbono orgânico total, pH e condutividade elétrica (CE) foram determinadas na fração dissolvida, enquanto a massa e as frações de parede celular (FPC) foram determinadas na fração particulada. A estabilização do pH das câmaras com folhas de T. ovata e S. officinarum ocorreram em meio básico (ca. 8 - 8,5) e próximo à neutralidade (ca. 7 - 7,5), respectivamente. Os valores de CE foram em média 1,6 vezes maiores nas incubações com folhas de T. ovata. A perda de massa não diferiu entre as espécies (média = 53,85%). No entanto, o coeficiente de decaimento foi maior para as folhas de S. officinarum (k4 = 0,007 dia-1) que para T. ovata (k4 = 0,005 dia-1). As perdas de massa da FPC (média = 50,16%) e seus respectivos coeficientes (0,0090 dia-1) foram similares. S. officinarum decompôs mais rapidamente devido às elevadas concentrações de compostos energéticos de interesse para a microbiota. A decomposição mais lenta de T. ovata pode ter ocorrido pela presença de compostos secundários com efeitos negativos sobre os micro-organismos.


Subject(s)
Water , Plant Leaves , Carbon-Carbon Lyases
5.
Chinese Journal of Biotechnology ; (12): 976-981, 2007.
Article in Chinese | WPRIM | ID: wpr-276176

ABSTRACT

Artemisinin,a new and a very potent antimalarial drug, is produced by the plant Artemisia annua L. with a very low yield ranging from 0.01% to 0.8% on a dry-weight basis. This makes artemisinin an expensive drug. Several studies reported chemical synthesis of the artemisinin, but none of them seems a viable economical alternative compared with the isolation of artemisinin from the plant. Hence, a higher artemisinin concentration in the plant is necessary for cheap antimalarial drug production. Many types of cyclic sesquiterpenes in Artemisia annua have been characterized to date, each derived from the common cyclic precursor FDP in a reaction catalyzed by a sesquiterpene synthase. Sesquiterpene synthases are widely regarded as the rate-determining regulatory enzymes in the pathways they participate, and a number of sesquiterpene synthases have been cloned from Artemisia annua up to now. This report is a brief review on the following sesquiterpene synthases: epi-cedrol synthase, amorpha-4,11-diene synthase, beta-caryophyllene synthase, (E)-beta-farnesene synthase, germacrene A synthase, as well as a new sesquiterpene synthase whose function remains largely unknown. The report is of help for a better understanding of metabolic engineering of Artemisia annua.


Subject(s)
Alkyl and Aryl Transferases , Genetics , Amino Acid Sequence , Antimalarials , Artemisia annua , Genetics , Artemisinins , Metabolism , Carbon-Carbon Lyases , Genetics , Cloning, Molecular , Escherichia coli , Genetics , Metabolism , Molecular Sequence Data , Recombinant Proteins , Genetics , Sesquiterpenes
6.
Indian J Exp Biol ; 1997 Jan; 35(1): 1-17
Article in English | IMSEAR | ID: sea-60077

ABSTRACT

The plant enzymes, 1-aminocyclopropane-1-carboxylic acid (ACC) synthase and ACC oxidase, catalyze essential steps in the biosynthesis of the phytohormone ethylene; the microbial enzyme ACC deaminase catalyses the hydrolytic cleavage of ACC, the immediate precursor of ethylene, and is therefore an inhibitor of ethylene biosynthesis. In this manuscript, the biochemical properties and mechanisms of these three enzymes and the genes that encode them are examined and compared. Despite the fact that ACC oxidase and ACC deaminase both act on the same substrate, i.e., ACC, these two enzymes and the mechanisms that they employ are quite different. Conversely, although ACC synthase catalyses the synthesis of ACC and ACC deaminase catalyses its hydrolysis, these enzymes share a number of important physical and biochemical properties.


Subject(s)
Amino Acid Oxidoreductases/metabolism , Amino Acid Sequence , Carbon-Carbon Lyases , Catalysis , Ethylenes/biosynthesis , Hydrolysis , Lyases/chemistry , Molecular Sequence Data
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