Examples of using Synthetase in English and their translations into Vietnamese
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The tyrocidine synthetases TycA, TycB, and TycC are encoded on the tyrocidine operon.
It is postulated that autoantibodies are formed against aminoacyl-tRNA synthetases.
Ligases(or synthetases)- couple the breakdown of a pyrophosphate bond in a nucleotide to the formation of new chemical bonds.
The polymyxins are produced by nonribosomal peptide synthetase systems in Gram-positive bacteria such as Paenibacillus polymyxa.
TycF has been identified as a thioesterase(TE) and is similar to other TEs inbacterial operons used for encoding peptide synthetases.
Borrelidin blocks the action of threonyl-tRNA synthetase, thereby preventing the amino acid L-threonine from linking to its tRNA.
A synthetase reaction(from the glutamine) forms the molecule glucosamine-6-phosphate, which then undergoes additional reactions in GAG synthesis.
Polymyxins are antibiotics produced by nonribosomal peptide synthetase systems in Gram-positive bacteria, such as Paenibacillus polymyxa.
Arts syndrome is a rare metabolic disorder that causes serious neurologicalproblems in males due to a malfunction of the PRPP synthetase 1 enzyme.
However, the precise function of these TEs remains unknown.[1]The size of the peptide synthetases corresponds to the amount of activation they carry out.
Genetic Conditions: More common in boys but occasionally occurring in girls, these conditions cause an over-production of uric acid(e.g. Lesch-Nyhan syndrome andPRPP synthetase overactivity).
During the III trimester of pregnancy, all prostaglandin synthetase inhibitors, including ketoprofen, can have toxic effects on the heart, lungs and kidneys of the fetus.
Arts syndrome is caused by a loss of function mutation in the PRPS1 gene.[1] The PRPS1 gene codes for the enzyme phosphoribosyl pyrophosphate synthetase 1 or PRPP synthetase 1.
Leukemic cells with low expression of asparagine synthetase have a reduced ability to synthesize L-asparagine, and therefore depend on an exogenous source of L-asparagine for survival.
Sulfonamide drugs are similar to PABA in their chemical structure, and their antibacterial activity is due to their ability to interfere with theconversion of PABA to folate by the enzyme dihydropteroate synthetase.
In humans, GARTfase is part of trifunctional enzyme which also includes glycinamide ribnucleotide synthase(GARS)and aminoimidazole ribonucleotide synthetase(AIRS). This protein(110kDa) catalyzes steps 2, 3 and 5 of de novo purine biosynthesis.
Sulfonamide drugs are similar to PABA in their chemical structure, and their antibacterial activity is due to their ability to interfere with theconversion of PABA to folate by the enzyme dihydropteroate synthetase.
Ribose-phosphate diphosphokinase(or phosphoribosyl pyrophosphate synthetase or ribose-phosphate pyrophosphokinase) is an enzyme that converts ribose 5-phosphate into phosphoribosyl pyrophosphate(PRPP).[1][2] It is classified under EC 2.7.6.1.
Tavaborole began its Phase 3 trials in December 2010[1] and was approved by the US FDA in July 2014.[2] Tavaborole inhibits an essential fungal enzyme,leucyl-tRNA synthetase, that is required for protein synthesis.
NAAG synthetase activity mediates the biosynthesis of NAAG from glutamate and NAA, but little is known about the mechanism or regulation of this enzyme, and no NAAG synthetase activity has been isolated in cell-free preparations.
In the guanine nucleotide pathway, there are 2 enzymes involved in converting IMP to GMP, namely IMP dehydrogenase(IMPD1), which catalyzes the oxidation of IMP to XMP,and GMP synthetase, which catalyzes the amination of XMP to GMP.[1].
Other names in common use include isoleucyl-tRNA synthetase, isoleucyl-transfer ribonucleate synthetase, isoleucyl-transfer RNA synthetase, isoleucine-transfer RNA ligase, isoleucine-tRNA synthetase, and isoleucine translase.
The mechanism of action is not fully understood, but nitrofurazone's antimicrobial properties are suspected to be due to the interference of DNA synthesis in the microorganism by inhibiting certain enzymes that are involved with glycolysis.[1][2] Other enzymes this may affect include, pyruvate dehydrogenase,citrate synthetase, malate dehydrogenase, glutathione reductase, and pyruvate decarboxylase.[1].
Diagnostic criteria require one ormore antisynthetase antibodies(which target tRNA synthetase enzymes), and one or more of the following three clinical features: interstitial lung disease, inflammatory myopathy, and inflammatory polyarthritis affecting small joints symmetrically.
The mechanism of action depends on competitive antagonism with para-aminobenzoic acid andinhibition of dihydropteroate synthetase activity, which in turn leads to impaired synthesis of dihydrofolic acid and as a result its active metabolite necessary for the synthesis of purine and pyrimidine.
AIR synthetase is found in both mitochondria and plastids; the mitochondrial form has 5 more amino acids than the plastid form.[1] The enzyme is encoded by a single gene in cowpeas despite the fact that it exists in different forms in plastids and mitochondria. This suggests that the different versions may be derived from a single transcript.
The systematic name of this enzyme class is xanthosine-5'-phosphate: L-glutamine amido-ligase(AMP-forming). Other names in common use include GMP synthetase(glutamine-hydrolysing), guanylate synthetase(glutamine-hydrolyzing), guanosine monophosphate synthetase(glutamine-hydrolyzing), xanthosine 5'-phosphate amidotransferase, and guanosine 5'-monophosphate synthetase.
Β-lactam synthetase is a 54.5 kDa protein that is encoded by orf3 of the clavulanic acid gene cluster, and shows similarity to asparagine synthase- Class B enzymes. The exact mechanism on how this enzyme works to synthesize the β-lactam is not proven, but is believed to occur in coordination with a CEA synthase and ATP.[10].
The first reaction of the carnitine shuttle is a two-stepprocess catalyzed by a family of isozymes of acyl-CoA synthetase that are found in the outer mitochondrial membrane, where they promote the activation of fatty acids by forming a thioester bond between the fatty acid carboxyl group and the thiol group of coenzyme A to yield a fatty acyl- CoA.[1].
Like other NRPs, polymyxins are assembled by synthetases with multiple modules, each containing a set of enzyme domains that sequentially operate on the growing chain by adding the next residue and extending the chain through peptide-bond formation and condensation reactions.