Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification
about
CharProtDB: a database of experimentally characterized protein annotationsCyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptidesSPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymesThe bacterial chemical repertoire mediates metabolic exchange within gut microbiomesThe Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether BondsX-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modificationX-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistryEmerging concepts promising new horizons for marine biodiscovery and synthetic biologyMetagenome mining reveals polytheonamides as posttranslationally modified ribosomal peptides.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.TIGRFAMs and Genome Properties in 2013.Using comparative genomics to drive new discoveries in microbiologyBiochemical and Spectroscopic Characterization of a Radical S-Adenosyl-L-methionine Enzyme Involved in the Formation of a Peptide Thioether Cross-Link.The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA PeptideGenome mining for ribosomally synthesized and post-translationally modified peptides (RiPPs) in anaerobic bacteria.PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway.Structure and biosynthesis of a macrocyclic peptide containing an unprecedented lysine-to-tryptophan crosslinkIn silico identification of bacteriocin gene clusters in the gastrointestinal tract, based on the Human Microbiome Project's reference genome databaseA prevalent peptide-binding domain guides ribosomal natural product biosynthesis.A comprehensive software suite for protein family construction and functional site prediction.New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqDPqqE from Methylobacterium extorquens AM1: a radical S-adenosyl-l-methionine enzyme with an unusual tolerance to oxygen.Mechanistic Enzymology of the Radical SAM Enzyme DesII.Stationary phase and nutrient levels trigger transcription of a genomic locus containing a novel peptide (TM1316) in the hyperthermophilic bacterium Thermotoga maritima.At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology.Insights into the catalysis of a lysine-tryptophan bond in bacterial peptides by a SPASM domain radical S-adenosylmethionine (SAM) peptide cyclase.Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.The PqqD homologous domain of the radical SAM enzyme ThnB is required for thioether bond formation during thurincin H maturation.Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in the mechanism of catalysis.Distribution and Genetic Diversity of Bacteriocin Gene Clusters in Rumen Microbial Genomes.Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides (RiPPs).Characterization of auxiliary iron-sulfur clusters in a radical S-adenosylmethionine enzyme PqqE from Methylobacterium extorquens AM1.Radical S-Adenosylmethionine Enzymes Involved in RiPP Biosynthesis.Structures of the peptide-modifying radical SAM enzyme SuiB elucidate the basis of substrate recognition.Spiroplasma affects host aphid proteomics feeding on two nutritional resources.X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC.The Radical SAM enzyme NirJ catalyzes the removal of two propionate side chains during heme d1 biosynthesis.C-C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products.
P2860
Q24621984-450DD693-8DD0-48A4-BF1B-455F596A56E7Q26738949-FFD783A1-CC17-4020-84E8-F65E3EB48590Q26865439-72BB7214-C5C3-4883-8FCD-F6699E096F7FQ27000963-F29B63DD-B072-4B6F-9D03-B686069C9E2FQ27313394-4A8BF9A8-677C-4FA3-9EC1-1C0CD4847D8CQ27678025-459DA08C-EE09-4568-8253-0C12BA147181Q27679985-9F21A490-160B-42CC-8D5A-0601F304C1B8Q28080553-04BB1A67-E349-49B1-8F01-436BD3F78764Q34033626-F1129264-3A3F-4BAE-B19B-576F155E17BFQ34312732-855822B2-D2B0-4F63-89E1-223302C1D85EQ34314590-0DF9F60B-33B3-47C0-90B1-222D3D05990EQ34459523-7E63177E-9240-4F8D-B8BB-980FB649D57FQ34519519-43B7A5F1-3171-456F-9D5F-7B5AA1179490Q34525745-4F594381-9EE6-42B4-833D-FE952EA33EC2Q35433857-D5AD132D-CFA0-4DD1-93F5-3DAC2DDBA8D5Q35608175-1D219B5F-683A-4ED7-8F0B-CF25A8F0D0D4Q35645486-827561A1-22B7-44CE-AEE8-20A433763493Q35777738-DD7E6DBC-703C-492A-AAEA-1B50EECBBD25Q35875602-19D03213-1D41-4E49-8DF1-0ECE71853822Q36275256-9E45F796-6E9D-416C-A4A7-A6EADFE20AE9Q36654180-906D7AB1-B794-4AE8-892D-843D43E42337Q36884755-729F097F-91E3-4673-B7D0-2D67646E6FAAQ36941648-AC3544B4-E5E0-46F0-9A4B-CDFD5D70BC2DQ37252787-46462E80-D875-4DD5-A54A-1E905D9C985BQ37263963-A103B820-863A-43C7-8D71-5BABA032D42BQ38613403-0526C18E-59AF-438A-AB30-CA7124E0BDA7Q38801328-0A0DBFC5-D812-41FC-96D5-DCB9F3394447Q39109460-73C3BF83-5AC2-4FF0-97D6-710D5F0BD265Q40887469-A5B3F9BF-0749-4CCB-82AC-8203E7FFC041Q41881940-0E8023BB-A464-4C03-BFC1-0B4E7C5AB386Q42144412-877710FF-3238-45DA-BD2A-E5FCFE648BABQ47103442-7558F3F4-0298-4725-8352-24D7BC4F29A8Q47107286-688C12EB-E1B6-452C-AF2B-A086E96EB3BEQ47685789-75A54D38-0F49-420E-8373-F5F917AB142FQ48091132-25ADCE96-DACB-4039-96BF-FF44440E3E20Q48095749-A9B01E3B-4791-4194-A738-155C5BBE8FF4Q48098700-DE8C2F31-5B79-4B97-9E91-2083B3735780Q48249211-B0D7D2BC-3DD2-407F-8D2B-159069ECDEC4Q50094595-424AA6BE-CD14-4B48-B2E7-4F6C99A0C9F5Q52326942-5FAA1318-FD2E-4496-97F8-70ADB614E7C7
P2860
Biological systems discovery in silico: radical S-adenosylmethionine protein families and their target peptides for posttranslational modification
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Biological systems discovery i ...... posttranslational modification
@ast
Biological systems discovery i ...... posttranslational modification
@en
type
label
Biological systems discovery i ...... posttranslational modification
@ast
Biological systems discovery i ...... posttranslational modification
@en
prefLabel
Biological systems discovery i ...... posttranslational modification
@ast
Biological systems discovery i ...... posttranslational modification
@en
P2860
P356
P1476
Biological systems discovery i ...... posttranslational modification
@en
P2093
Malay Kumar Basu
P2860
P304
P356
10.1128/JB.00040-11
P407
P577
2011-04-08T00:00:00Z