CMMC_Bile_Salt_Hydrolase_Rxn_5.1
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): No Species
SUBMITTER: 
Pieter C. Dorrestein
PROVIDER: MSV000094811 | MassIVE | Mon May 20 16:10:00 BST 2024
REPOSITORIES: MassIVE
Similar Datasets
Project description:MS/MS fragmentation data of BSH enzyme assay of cholic glycine with a mix of 10 amino acids (Phenylalanine, Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic Acid, Glutamine, Histidine, and Isoleucine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-05-07 | MSV000094707 | MassIVE
Project description:MS/MS fragmentation data of BSH enzyme assay of cholic glycine with a mix of 10 amino acids (Phenylalanine, Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic Acid, Glutamine, Histidine, and Isoleucine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-04-04 | MSV000094468 | MassIVE
Project description:MS/MS fragmentation data of BSH enzyme assay of taurylcholic acid with a mix of 10 amino acids (Phenylalanine, Alanine, Arginine, Asparagine, Cysteine, Glutamine, Histidine, Methionine, Lysine, and Isoleucine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-05-20 | MSV000094811 | GNPS
Project description:MS/MS fragmentation data of BSH enzyme assay of taurylcholic acid with a mix of 10 amino acids (Phenylalanine, Alanine, Arginine, Asparagine, Cysteine, Glutamine, Histidine, Methionine, Lysine, and Isoleucine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-05-17 | MSV000094789 | GNPS
Project description:MS/MS fragmentation data of BSH enzyme assay of cholic glycine with a mix of 10 amino acids (Phenylalanine, Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic Acid, Glutamine, Histidine, and Isoleucine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-05-07 | MSV000094707 | GNPS
Project description:MS/MS fragmentation data of BSH enzyme assay of cholic glycine with a mix of 10 amino acids (Phenylalanine, Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic Acid, Glutamine, Histidine, and Isoleucine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-04-04 | MSV000094468 | GNPS
Project description:Objective: Insulin regulates amino acid metabolism. We investigated whether glycemia and 43 genetic risk variants for hyperglycemia/type 2 diabetes affect amino acid levels in a large population-based cohort. Subjects and Methods: A total of 9,371 non-diabetic or newly-diagnosed type 2 diabetic Finnish men from the population-based METSIM Study were studied. Proton NMR spectroscopy was used to measure plasma levels of 8 amino acids. Genotyping of 42 SNPs and mRNA microarray analysis from 200 subcutaneous adipose tissue samples were performed. Results: Increasing fasting and/or 2-hour plasma glucose levels were associated with increasing levels of alanine, valine, leucine, isoleucine, phenylalanine and tyrosine, and decreasing levels of histidine and glutamine. We also found significant correlations between insulin sensitivity (Matsuda ISI) and expression of genes regulating amino acid metabolism. Only one SNP (rs780094 in GCKR) of the 42 risk SNPs for type 2 diabetes or hyperglycemia was significantly associated with the levels of alanine, isoleucine, and glutamine. Conclusions : We observed that the levels of branched-chain, aromatic amino acids and alanine increased and the levels of glutamine and histidine decreased with increasing glycemia. These associations seemed to be mediated by insulin resistance, at least in part. GCKR rs780094 was significantly associated with several amino acids. Total RNA was obtained from subcutaneous fat biopsies from 200 people participating in the METSIM study (4 samples were replicated for a total of 204 arrays).
2012-04-01 | E-GEOD-32512 | biostudies-arrayexpress
Project description:Objective: Insulin regulates amino acid metabolism. We investigated whether glycemia and 43 genetic risk variants for hyperglycemia/type 2 diabetes affect amino acid levels in a large population-based cohort. Subjects and Methods: A total of 9,371 non-diabetic or newly-diagnosed type 2 diabetic Finnish men from the population-based METSIM Study were studied. Proton NMR spectroscopy was used to measure plasma levels of 8 amino acids. Genotyping of 42 SNPs and mRNA microarray analysis from 200 subcutaneous adipose tissue samples were performed. Results: Increasing fasting and/or 2-hour plasma glucose levels were associated with increasing levels of alanine, valine, leucine, isoleucine, phenylalanine and tyrosine, and decreasing levels of histidine and glutamine. We also found significant correlations between insulin sensitivity (Matsuda ISI) and expression of genes regulating amino acid metabolism. Only one SNP (rs780094 in GCKR) of the 42 risk SNPs for type 2 diabetes or hyperglycemia was significantly associated with the levels of alanine, isoleucine, and glutamine. Conclusions : We observed that the levels of branched-chain, aromatic amino acids and alanine increased and the levels of glutamine and histidine decreased with increasing glycemia. These associations seemed to be mediated by insulin resistance, at least in part. GCKR rs780094 was significantly associated with several amino acids.
2012-04-02 | GSE32512 | GEO
Project description:MS/MS fragmentation data of 2 BSH enzyme assays. One with taurylcholic acid and the other with glycocholic acid each with a mix of 43 amino compounds (Asparagine, Aspartic Acid, L-Glutamic Acid, Glutamine, Methionine, 4-aminophenol, Tryptamine, B-Alanine, L-Carnosine, Allantoin, 2-Phenylglycine, L-aspartyl-L-phenylalanine methyl ester, Isoniazid, DL-Proline, Creatine, Histamine. L-Alanine, L-Arginine, L-Cysteine, L-Leucine, Lysine, Phenylalanine, Serine, Tryptophan, Valine, 1,3-Diaminopropane, L-citrulline, 5-Aminovaleric Acid, Dopamine, Serotonin, Histidine, L-Homoserine, L(+)-Ornithine, gamma-Aminobutyric acid, L-Glutathione (oxidized form), trans-4-Hydroxy-L-proline, L(+)-Homoarginine, Glycyl-L-Valine, L-2-Aminoadipic Acid, L-Glutathione reduced, 3-methoxytyramine, Threonine, and Tyramine) acquired on Q Exactive - with chromatographic separation on a Phenomenex polar C18 column.
2024-07-02 | MSV000095220 | GNPS
Project description:To ensure that the pool of precursor amino acids utilized for protein synthesis is completely labeled prior to the first labeling time-point, we conducted an isotopomer analysis. After adaption to media, cells were plated at a density of 500,000 cells per 10 cm plate. 8 days after plating, the confluent quiescent cultures were switched to 15N labeling medium. Cells were collected after 0h, 6h, 1d, 2d, 4d of labeling, washed with PBS and cell pellets were frozen prior to further analysis. 15N labeling medium was made from “Cell free” Amino Acid Mix (20AA, U-15N, 96-98%)(Cambridge Isotope Laboratories) and supplemented with 15% dialyzed fetal bovine serum (Thermo Scientific), 100U/mL penicillin, 100U/mL streptomycin. 1g is used for making 702mL labeling medium. The final amino acids concentrations in 15N labeling medium are as following: Alanine: 0.1140 g/L, Arginine: 0.0499 g/L, Asparagine: 0.0940 g/L, Aspartic acid: 0.1353 g/L, Cystine: 0.01140 g/L, Glutamic acid: 0.1852 g/L, Glutamine: 0.0869 g/L, Glycine: 0.0698 g/L, Histidine: 0.0157 g/L, Isoleucine: 0.0698 g/L, Leucine: 0.1211 g/L, Lysine: 0.0527 g/L, Methionine: 0.0228 g/L, Phenylalanine: 0.0541 g/L, Proline: 0.0299 g/L, Serine: 0.0541 g/L, Threonine: 0.0741 g/L, Tryptophan: 0.0456 g/L, Tyrosine: 0.0613g/L, Valine: 0.0798 g/L. LC-MS/MS and quantitative analysis of isotopic envelopes and 15N incorporation of peptides was conducted as described in (Zhang et al., 2014). The data indicate that when exposed to fully 15N-labeled media (where all 20 natural amino acids are isotopically labeled), the fraction of proteins that are synthesized within the first day are almost fully labeled. Thus, the extent of fractional labeling is almost exclusively influenced by the kinetics of protein turnover rather than amino acid uptake and recycling within the cell. Table of files Cells Time points Labeling Fractionation Raw Data Filenames Wildtype 0d, 1d,2d,4d,7d13C 6Lys, 6Arg& 15N No 0d.raw 1d.raw 2d.raw 4d.raw 7d.raw
2016-06-14 | PXD003559 | Pride