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28 results for “transaminase”
Development of an Amine Transaminase-Lipase Cascade for Chiral Amide Synthesis under Flow Conditions
<p>The use of multienzymatic systems has gained increasing attention as a method of choice for complex (asymmetric) syntheses. Incompatibilities between substrates, reagents and/or enzymes in one-pot batch conditions can hamper the applicability of a pursued cascade, so the use of flow systems provide useful synthetic solutions. The implementation of immobilised enzymes in continuous flow reactors allows the compartmentalisation and segregation of the enzymes in separate reactors, leading to otherwise disfavoured reaction cascades. Here, an amine transaminase and a lipase have been immobilised on polymer-coated controlled porosity glass carrier materials and studied for the first time together in the transamination of a prochiral ketone followed by acylation of the corresponding chiral amine in flow mode, two incompatible transformations under batch. Thus, the preparation of (<em>R</em>)-<em>N</em>-(1-phenoxypropan-2-yl)acetamide was accomplished after optimisation of the reaction conditions.</p>
FTIR Microscopy for Direct Observation of Conformational Changes on Immobilized ω-Transaminase: Effect of Water Activity and Organic Solvent on Biocatalyst Performance
<p>Enzyme immobilization is a key strategy to expand the scope of enzyme applications and to enable the recycling of biocatalysts, resulting in greener and more cost-efficient processes. The full exploitation of the technology advantages is strictly connected to the optimal selection of the carriers and the rational development of the immobilization protocol. The present study achieved such objectives by investigating the activity of a ω-transaminase in organic solvent (toluene) upon immobilization on commercially controlled porosity glass carriers (EziG™) with diverse porosity and surface functionalization. In addition to more conventional wet-chemistry approaches and confocal microscopy, infrared microspectroscopy and imaging were exploited to highlight the enzyme distribution in a label-free manner and provide details on the immobilized enzyme's conformation with respect to the native form. Contrary to what could be expected, the highest activity of the enzyme in organic solvent was achieved for the immobilization protocol on the most hydrophilic support that more severely affects the enzyme secondary structure, promoting a beta-sheet rich folding. Experimental data show that values of water activity above 0.90 in the reaction system had a positive effect on the efficiency of the transaminase reaction. The present study represents the first example of rational development of immobilization protocols relying on direct observation of the enzyme conformation upon immobilization, shedding light on the mutual interaction between the diverse process parameters and the carrier properties.</p>
The Role of Buffer, Pyridoxal 5'-Phosphate and Light on the Stability of the Silicibacter Pomeroyi Transaminase
<p>Transaminases are pyridoxal 5’-phosphate (PLP)-dependent enzymes that transfer amino-functions. The transaminase from <em>Silicibacter pomeroyi</em> (SpATA) exhibits a broad substrate spectrum. In this work we examined the effect of different conditions (light, buffer and PLP-concentration) on the stability of SpATA, as well as the causes for these effects. The enzyme was stored either in TRIS or CHES with 0–10 mM added PLP at 22 °C. The samples were either kept dark or they were exposed to light. The results show that invariably, all samples kept in darkness exhibited longer half-life times than the ones exposed to light. An increase in the half-life from 8 h to 720 h could be achieved solely by keeping the sample dark. Especially samples in CHES buffer inactivated faster in light the more PLP was present, due to the degradation of PLP. In TRIS however, an imine-bond between TRIS and PLP protects PLP from degradation.</p>
A Multiplex Assay to Assess the Transaminase Activity toward Chemically Diverse Amine Donors
<p>The development of methods to engineer and immobilize amine transaminases (ATAs) to improve their functionality and operational stability is gaining momentum. The quest for robust, fast, and easy-to-use methods to screen the activity of large collections of transaminases, is essential. This work presents a novel and multiplex fluorescence-based kinetic assay to assess ATA activity using 4-dimethylamino-1-naphthaldehyde as an amine acceptor. The developed assay allowed us to screen a battery of amine donors using free and immobilized ATAs from different microbial sources as biocatalysts. As a result, using chromatographic methods, 4-hydroxybenzylamine was identified as the best amine donor for the amination of hydroxy methyl furfural. Finally, we adapted this method to determine the apparent Michaelis-Menten parameters of a model immobilized ATA at the microscopic (single-particle) level. Our studies promote the use of this multiplex, multidimensional assay to screen ATAs for further improvement.</p>
Biosynthesis of Furfurylamines in Batch and Continuous Flow by Immobilized Amine Transaminases
<p>Building blocks with amine functionality are crucial in the chemical industry. Biocatalytic syntheses and chemicals derived from renewable resources are increasingly desired to achieve sustainable production of these amines. As a result, renewable materials such as furfurals, especially furfurylamines like 5-(hydroxymethyl)furfurylamine (HMFA) and 2,5-di(aminomethyl)furan (DAF), are gaining increasing attention. In this study, we identified four different amine transaminases (ATAs) that catalyze the reductive amination of 5-(hydroxymethyl)furfural (HMF) and 2,5-diformylfuran (DFF). We successfully immobilized these ATAs on glutaraldehyde-functionalized amine beads using multiple binding and on amine beads by site-selective binding of the unique Cα-formylglycine within an aldehyde tag. All immobilized ATAs were efficiently reused in five repetitive cycles of reductive amination of HMF with alanine as co-substrate, while the ATA from <em>Silicibacter pomeroyi</em> (ATA-Spo) also exhibited high stability for reuse when isopropylamine was used as an amine donor. Additionally, immobilized ATA-Spo yielded high conversion in the batch syntheses of HMFA and DAF using alanine (87% and 87%, respectively) or isopropylamine (99% and 98%, respectively) as amine donors. We further demonstrated that ATA-Spo was effective for the reductive amination of HMF with alanine or isopropylamine in continuous-flow catalysis with high conversion up to 12 days (48% and 41%, respectively).</p>
D-Glu hydrolysis in the active site of the AmicoTA, a transaminase from the Gram-negative mesophilic bacterium Aminobacterium colombiense
<p>500 frames from the QM(PBE0-D3/6-31G**)/MM molecular dynamic trajectory in the transition state region. The external potential is centered at 3.9 Å of the collective variable (a sum of the distances between the hydrogen atom of the protonated amino group and an oxygen atom the α-carboxylate group of the substrate and between the nitrogen atom of the substrate and a C4´ atom of PLP).</p> <p>In the PDB file the QM atoms have beta=1 and MM beta=0.</p>
A Study of IDN-6556 in Subjects With NAFLD and Raised Transaminases
ClinicalTrials.gov study NCT02077374. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Evaluation of Chronic HBV Patients w/Evidence of HBV Replication and Normal or Minimally Elevated Liver Transaminases.
ClinicalTrials.gov study NCT00263614. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Prevalence of elevated liver transaminases and their relationship with alcohol use in people living with HIV on anti-retroviral therapy in Uganda
Open the record for dataset details and reuse information.
A Quality of Life Study of Peginterferon-Alfa-2a Plus Ribavirin in Participants With Chronic Hepatitis C and Persistently Normal Alanine Transaminase (ALT) Levels
ClinicalTrials.gov study NCT02726022. IPD Sharing: Not stated. Countries: 1. Publications: 0.
Evaluation of Antiviral Indications on Chronic HBV Infection With Different Transaminase Levels
ClinicalTrials.gov study NCT03740789. IPD Sharing: Not stated. Countries: 1. Publications: 0.
Efficacy of Montelukast in Preventing Transaminase Elevation in Adult Dengue Patients
ClinicalTrials.gov study NCT06747130. IPD Sharing: UNDECIDED. Countries: 1. Publications: 0.
To Evaluate the Efficacy of DDB/Garlic Oil in Patients With Elevated Transaminase Chronic Liver Disease
ClinicalTrials.gov study NCT02347319. IPD Sharing: Not stated. Countries: 1. Publications: 0.
Study to Evaluate the Treatment for Chronic Hepatitis C With Normal Transaminases in HIV Positive Patients
ClinicalTrials.gov study NCT01684787. IPD Sharing: Not stated. Countries: 1. Publications: 0.
Silencing alanine transaminase 2 in diabetic liver attenuates hyperglycemia by reducing gluconeogenesis from amino acids
GEO Series GSE199975. Mus musculus. 24 samples. Type: Expression profiling by high throughput sequencing.
Deletion of the Saccharomyces cerevisiae ARO8 gene, encoding an aromatic amino acid transaminase, enhances phenylethanol production from glucose
GEO Series GSE52256. Saccharomyces cerevisiae. 4 samples. Type: Expression profiling by array.
The transaminase-ω-amidase pathway is a redox switch in glutamine metabolism that generates α-ketoglutarate [RNA-seq_NIT2-GLS1-KO]
GEO Series GSE302820. Homo sapiens. 16 samples. Type: Expression profiling by high throughput sequencing.
Role of Branched Chain Amino Acid Transaminase 1 (BCAT1) in Acute Myeloid Leukemia [methylation_HL60_BCAT1-OE_20weeks]
GEO Series GSE100780. Homo sapiens. 4 samples. Type: Methylation profiling by genome tiling array.
Role of Branched Chain Amino Acid Transaminase 1 (BCAT1) in Acute Myeloid Leukemia
GEO Series GSE100784. Homo sapiens. 56 samples. Type: Expression profiling by array; Methylation profiling by genome tiling array.
Role of Branched Chain Amino Acid Transaminase 1 (BCAT1) in Acute Myeloid Leukemia [methylation_HL60_BCAT1-OE_10weeks]
GEO Series GSE100779. Homo sapiens. 6 samples. Type: Methylation profiling by genome tiling array.
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