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. 2010 Jan;5(8):340-344.
doi: 10.1128/microbe.5.340.1.

N ε-Lysine Acetylation Control Conserved in All Three Life Domains: The relative simplicity of studying microbes could prove critical for understanding this posttranslational modification system

Jorge C Escalante-Semerena  1
Affiliations

N ε-Lysine Acetylation Control Conserved in All Three Life Domains: The relative simplicity of studying microbes could prove critical for understanding this posttranslational modification system

Jorge C Escalante-Semerena. Microbe Wash DC. 2010 Jan.
No abstract available

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Figures

FIGURE 1
FIGURE 1
Metabolic fates of acetyl-CoA.
FIGURE 2
FIGURE 2
Nε-Lysine acetylation controls the activity of acetyl-CoA synthetase. The two steps of the reaction catalyzed by the acetyl-coenzyme A synthetase (Acs) enzyme is shown at the bottom of the figure. Each color represents a different conformation state of Acs. Green, Acs in the conformation that catalyzes the formation of the acyl-AMP intermediate; red, Acs in the conformation that converts acyl-AMP to acyl-CoA; gray-shaded hexagon, apo Acs in the conformation with the side chain of a critical Lys residue exposed; colored hexagon, inactive acetylated Acs; blue, acetylated Acs with ATP and acetate bound to the active site.
FIGURE 3
FIGURE 3
Putative acylation motif found in members of the AMP-forming family of enzymes. The following are enzymes present in E. coli K-12, and S. enterica serovar Typhimurium LT2: Acs, acetyl-CoA synthetase; PrpE, propionyl-CoA synthetase; Aas, acyl-[acyl carrier protein] synthetase/2-acylglycerophosphoethanolamine acyltramnsferase; FadD, long-chain, fatty acid:CoA ligase; EntE, enterobactin synthase subunit E; EntF, enterobactin synthase, subunit F; CaiC, crotonobetaine/carnitine:CoA ligase; YdiD (FadK, short-chain acid:CoA ligase. GrsA, gramicidin synthetase from Bacillus brevis; hmAcs2A, human mitochondrial acetyl-CoA synthetase 2A; BadA, bezoate:CoA ligase from Rhodopseudomonas palustris. The lower part of the figure shows the frequency at which a specific residue is found within the motif.
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