about
The methylthiolation reaction mediated by the Radical-SAM enzymesPost-translational Modification of Ribosomal Proteins: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF RimO FROM THERMOTOGA MARITIMA, A RADICAL S-ADENOSYLMETHIONINE METHYLTHIOTRANSFERASETwo Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferasesCo-opting sulphur-carrier proteins from primary metabolic pathways for 2-thiosugar biosynthesisMitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes.The ISC [corrected] proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae.Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNAC-S bond cleavage by a polyketide synthase domain.A bioinspired and biocompatible ortho-sulfiliminyl phenol synthesis.A biosynthetic pathway for BE-7585A, a 2-thiosugar-containing angucycline-type natural product.Mechanistic studies of the biosynthesis of 2-thiosugar: evidence for the formation of an enzyme-bound 2-ketohexose intermediate in BexX-catalyzed reactionIron-catalyzed aerobic difunctionalization of alkenes: a highly efficient approach to construct oxindoles by C-S and C-C bond formation.Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediatetRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme diiron monooxygenase.(E)-3-(4-Methyl-phen-yl)-1-(1,3-thia-zol-2-yl)prop-2-en-1-one.Accessing Ni(III)-thiolate versus Ni(II)-thiyl bonding in a family of Ni-N2S2 synthetic models of NiSODAn embarrassment of riches: the enzymology of RNA modification.Photochemistry of furyl- and thienyldiazomethanes: spectroscopic characterization of triplet 3-thienylcarbeneMolecular architectures and functions of radical enzymes and their (re)activating proteins.Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis.Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway.Iron regulation through the back door: iron-dependent metabolite levels contribute to transcriptional adaptation to iron deprivation in Saccharomyces cerevisiae.Cyanomethylidyne: a reactive carbyne radical.Density functional theory calculations on the active site of biotin synthase: mechanism of S transfer from the Fe(2)S(2) cluster and the role of 1st and 2nd sphere residues.Identification and characterization of a welwitindolinone alkaloid biosynthetic gene cluster in the stigonematalean Cyanobacterium Hapalosiphon welwitschii.Expression, crystallization and preliminary crystallographic analysis of SufE (XAC2355) from Xanthomonas axonopodis pv. citri.9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses.The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster.Hydrogen transfer in SAM-mediated enzymatic radical reactions.MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA.The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly.Enzymatic mechanisms of biological magnetic sensitivity.Three-component difunctionalization of alkenes leading to β-acetamido sulfides and β-acetoxy sulfides.-Butylphenolic Derivatives from -A Case of BioconversionEnzymatic mechanisms of biological magnetic sensitivity: nuclear spin effects
P2860
Q26822523-B7952896-9617-4270-A2A3-864B107F22ECQ27646586-05D7C42C-2729-46E4-9934-7423EBC0D0E8Q27677136-8A5906C4-AC63-46E3-AA47-3DF46487CCF2Q27683702-0906B501-E324-4B1C-A070-B93D23E5F1AAQ27937403-8208DD8F-A57C-4002-905B-0308AE400764Q27938255-C5DD702F-B290-4D6C-8E85-D90CFEA5E04CQ28118753-DAA4074E-E434-42FF-B9FA-5EFBC726076AQ30984909-BBC0391B-0E16-44BA-8183-12C6AF2F0CD7Q33827130-8815BF43-5374-4C91-BB4D-D61CC4E18716Q33897077-5E5FBCD9-87EA-41FA-ACD2-9B0B312BFC1FQ34284443-05B1BF86-9C17-4B5C-8482-F52FD52B7125Q35119109-4AF8647D-74BB-4CF2-9C64-B0523D6B8F45Q35824616-A1C2D647-C966-410D-8B4A-C3AFF4185CB5Q35941232-96D524C9-4D43-431D-B306-6636BAA5651AQ36046701-9653C2F3-DDA3-40E3-B770-8B1F6043AB33Q36243050-3CA58F4D-CD91-4D82-8FD3-C37B3EFE2987Q37092594-0D9D0BDE-6CC7-4039-8E01-B10340692E1BQ37715617-F2A43070-4FD2-45B2-A755-C787AF4B00C5Q38564134-22D4DBD7-D8D5-4410-BE52-83DB7AE074E2Q38951352-71E0FCFF-1A15-4DEE-95F0-440E4B13383BQ39119961-C17AE655-3C68-4A27-9D6B-3EB2B7878226Q39605933-9D877E63-745A-4176-A7BF-C40E66386180Q40346057-DD2C6EA4-4642-421B-B5F9-D8AF5941CD12Q40540646-4778BA66-6489-434B-93FA-B6336EE37673Q41823506-18331D70-B251-42F5-AFEE-279AFDF5116BQ42010523-1291EA8D-6676-416C-A076-73559842CECFQ42274127-716B1481-CB82-42F0-9C1C-5829720E19B8Q43006437-EF4956B4-0611-4AC3-A208-C729F8D24F55Q43018711-429C5AEE-5F76-42CB-921E-53838A4BADDEQ44379183-01A9569F-034A-459C-9E23-871BEC99DC65Q45038651-B211D9CE-2CFD-4534-BC6C-4791CDAB280CQ46149437-F98B756E-50CB-439F-B55E-01A70E66B896Q48113949-ACD7BDAD-5C6B-42B8-ACAA-38C601168975Q48258188-F64A8109-DC26-47E1-8543-EB9DB1004667Q58692760-68B71EC8-0CF4-4BAA-8DEE-8D99773F1D79Q59329721-EB6110FB-0869-49EE-946A-60844D6F0600
P2860
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Biological radical sulfur insertion reactions.
@ast
Biological radical sulfur insertion reactions.
@en
type
label
Biological radical sulfur insertion reactions.
@ast
Biological radical sulfur insertion reactions.
@en
prefLabel
Biological radical sulfur insertion reactions.
@ast
Biological radical sulfur insertion reactions.
@en
P356
P1433
P1476
Biological radical sulfur insertion reactions.
@en
P2093
Etienne Mulliez
Sandrine Ollagnier-de-Choudens
P304
P356
10.1021/CR020427J
P577
2003-06-01T00:00:00Z