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A Toxin Involved in Salmonella Persistence Regulates Its Activity by Acetylating Its Cognate Antitoxin, a Modification Reversed by CobB Sirtuin Deacetylase.In Bacillus subtilis, the SatA (formerly YyaR) acetyltransferase detoxifies streptothricin via lysine acetylation.The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle.In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and Nε -lysine acetylation.Facile isolation of α-ribazole from vitamin B12 hydrolysates using boronate affinity chromatography.Small-Molecule Acetylation Controls the Degradation of Benzoate and Photosynthesis in Rhodopseudomonas palustrisA New Class of EutT ATP:Co(I)rrinoid Adenosyltransferases Found in Listeria monocytogenes and Other Firmicutes Does Not Require a Metal Ion for ActivityThe Methanosarcina mazei MM2060 Gene Encodes a Bifunctional Kinase/Decarboxylase Enzyme Involved in Cobamide BiosynthesisMutational and Functional Analyses of Substrate Binding and Catalysis of the Listeria monocytogenes EutT ATP:Co(I)rrinoid AdenosyltransferaseSpectroscopic Study of the EutT Adenosyltransferase from Listeria monocytogenes: Evidence for the Formation of a Four-Coordinate Cob(II)alamin IntermediateRhodobacterales use a unique L-threonine kinase for the assembly of the nucleotide loop of coenzyme B12A New Class of Phosphoribosyltransferases Involved in Cobamide Biosynthesis Is Found in Methanogenic Archaea and CyanobacteriaNew AMP-forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylationInsights into the Function of the N-Acetyltransferase SatA That Detoxifies Streptothricin in Bacillus subtilis and Bacillus anthracisThe l-Thr Kinase/l-Thr-Phosphate Decarboxylase (CobD) Enzyme from Methanosarcina mazei Gö1 Contains Metallocenters Needed for Optimal ActivitySmall-Molecule Acetylation by GCN5-Related N-Acetyltransferases in BacteriaStaphylococcus aureus modulates the activity of acetyl-Coenzyme A synthetase (Acs) by sirtuin-dependent reversible lysine acetylation
P50
Q33741257-4866A511-5F9D-42F6-B78D-9D767B721296Q38607659-0CF6B331-EBE1-42B7-9026-8B8F65899F4CQ47148388-65A8789C-BDB7-4FB4-B299-A86B0752C210Q47266049-AA7B4E8D-2BCE-4A2B-86A4-07BEFB9B486DQ54108358-77BE0C7E-40D2-4B51-9DEC-3D9FF00F7735Q57459051-BB121A46-D4A4-4EFC-9564-261D1A33EDC1Q58773271-021D6DD8-BBFE-4F92-A0D5-6A91B6FDD615Q89292786-2F6EF9A6-E670-42E7-A59B-E18178BB2977Q89996244-F3122436-02D4-4BF0-AD74-45A10F989000Q90713157-E9EA66B8-1EBF-4494-850C-86149A6DA949Q90883900-29A2975C-6C6B-4948-A06F-8B80A3A9CFE3Q91034442-FD70CFFC-B382-4A1C-B729-F22C6925654AQ91065311-A9689AFA-AC99-4F28-86A7-D99DFA331A54Q91116476-01DDEB3D-1682-4977-BA4B-A4B7F972D76CQ91575995-E2202A6A-20AA-41DC-A59B-CF9FC0EF050AQ91968950-44E47797-0510-4D61-8EE9-1DCFC2FC41CAQ92111816-FCDCFCDB-0F0D-4717-9953-733F9CF3580A
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description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Jorge C Escalante-Semerena
@ast
Jorge C Escalante-Semerena
@en
Jorge C Escalante-Semerena
@es
Jorge C Escalante-Semerena
@fr
Jorge C Escalante-Semerena
@nl
Jorge C Escalante-Semerena
@sl
type
label
Jorge C Escalante-Semerena
@ast
Jorge C Escalante-Semerena
@en
Jorge C Escalante-Semerena
@es
Jorge C Escalante-Semerena
@fr
Jorge C Escalante-Semerena
@nl
Jorge C Escalante-Semerena
@sl
prefLabel
Jorge C Escalante-Semerena
@ast
Jorge C Escalante-Semerena
@en
Jorge C Escalante-Semerena
@es
Jorge C Escalante-Semerena
@fr
Jorge C Escalante-Semerena
@nl
Jorge C Escalante-Semerena
@sl
P106
P21
P31
P496
0000-0001-7428-2811