Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism.

Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism.

Item
http://www.wikidata.org/entity/Q35370523
Bacterial GCN5-Related N-Acetyltransferases: From Resistance to RegulationAcylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic StressBroad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificityThe metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7Distinct type I and type II toxin-antitoxin modules control Salmonella lifestyle inside eukaryotic cells.Reversible lysine acetylation is involved in DNA replication initiation by regulating activities of initiator DnaA in Escherichia coli.In Bacillus subtilis, the SatA (formerly YyaR) acetyltransferase detoxifies streptothricin via lysine acetylation.Bacterial protein acetylation: new discoveries unanswered questions.The acetylation motif in AMP-forming Acyl coenzyme A synthetases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris.Novel protein acetyltransferase, Rv2170, modulates carbon and energy metabolism in Mycobacterium tuberculosisAcetate metabolism regulation in Escherichia coli: carbon overflow, pathogenicity, and beyond.Metabolic defence against oxidative stress: the road less travelled so far.The Protein Acetyltransferase PatZ from Escherichia coli Is Regulated by Autoacetylation-induced Oligomerization.Cyclic AMP-dependent protein lysine acylation in mycobacteria regulates fatty acid and propionate metabolism.A positive selection approach identifies residues important for folding of Salmonella enterica Pat, an N(ε)-lysine acetyltransferase that regulates central metabolism enzymes.Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans.In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and Nε -lysine acetylation.
P2860

Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric N(ε)-lysine acetyltransferase involved in carbon and energy metabolism.

Item
http://www.wikidata.org/entity/Q35370523
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին 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
Biochemical and thermodynamic ...... carbon and energy metabolism.
@ast
Biochemical and thermodynamic ...... carbon and energy metabolism.
@en
type
label
Biochemical and thermodynamic ...... carbon and energy metabolism.
@ast
Biochemical and thermodynamic ...... carbon and energy metabolism.
@en
prefLabel
Biochemical and thermodynamic ...... carbon and energy metabolism.
@ast
Biochemical and thermodynamic ...... carbon and energy metabolism.
@en
P1433
P1476
P2093
P2860
P31
P356
P433
P478
P577
P5875
P698
P921
P932
P356
P1433
P1476
Biochemical and thermodynamic ...... carbon and energy metabolism.
@en
P2093
P2860
P31
P356
P433
P478
P577
P5875
P698
P921
P932