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Literature summary for 2.3.1.48 extracted from

  • Albaugh, B.N.; Kolonko, E.M.; Denu, J.M.
    Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex (2010), Biochemistry, 49, 6375-6385.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.48

Protein Variants

Protein Variants Comment Organism
D287A/D288A mutation does not substantially change the shape of the kcat-pH profile, suggesting these conserved residues do not function as base catalysts for histone acetylation Saccharomyces cerevisiae
D287N mutation does not substantially change the shape of the kcat-pH profile, suggesting these conserved residues do not function as base catalysts for histone acetylation Saccharomyces cerevisiae
D288N mutation does not substantially change the shape of the kcat-pH profile, suggesting these conserved residues do not function as base catalysts for histone acetylation. Mutant reveals a dramatic 1000fold decrease in kcat/Km for acetyl-CoA Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
CoA CoA binds competitively with acetyl-CoA Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0003
-
 acetyl-CoA wild-type, pH 7.5, 25°C Saccharomyces cerevisiae
0.00049
-
 acetyl-CoA mutant D288N, pH 7.5, 25°C Saccharomyces cerevisiae
0.0007
-
 acetyl-CoA mutant D287N, pH 7.5, 25°C Saccharomyces cerevisiae
0.007
-
 histone H3 wild-type, pH 7.5, 25°C Saccharomyces cerevisiae
0.044
-
 histone H3 tail peptide mutant D287A/D288A, pH 7.5, 25°C Saccharomyces cerevisiae
0.055
-
 histone H3 tail peptide mutant D288N, pH 7.5, 25°C Saccharomyces cerevisiae
0.062
-
 histone H3 tail peptide mutant D287N, pH 7.5, 25°C Saccharomyces cerevisiae
0.112
-
 histone H3 tail peptide wild-type, pH 7.5, 25°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q07794
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine sequential mechanism in which acetyl-CoA and H3 bind to a complex of isoform Rtt109 and histone chaperone Vps75 without obligate order, followed by the direct attack of the unprotonated epsilon-amino group on acetyl-CoA, transferring the acetyl-group to H3 lysine residues The chemical attack of substrate lysine on the bound acetyl-CoA is the rate-limiting step of catalysis Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + histone H3
-
 Saccharomyces cerevisiae CoA + acetylhistone H3
-
 ?
acetyl-CoA + histone H3 tail peptide H3 peptide substrate, amino acid sequence ARTKQTARKSTGGKAPRKQL Saccharomyces cerevisiae CoA + acetylhistone H3 peptide
-
 ?

Subunits

Subunits Comment Organism
More isoform Rtt109 and histone chaperone Vps75 form a stable complex with nanomolar binding affinity Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Rtt109
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0011
-
 histone H3 tail peptide mutant D287A/D288A, pH 7.5, 25°C Saccharomyces cerevisiae
0.0021
-
 histone H3 tail peptide mutant D288N, pH 7.5, 25°C Saccharomyces cerevisiae
0.0028
-
 acetyl-CoA mutant D288N, pH 7.5, 25°C Saccharomyces cerevisiae
0.0087
-
 histone H3 tail peptide mutant D287N, pH 7.5, 25°C Saccharomyces cerevisiae
0.012
-
 acetyl-CoA mutant D287N, pH 7.5, 25°C Saccharomyces cerevisiae
0.11
-
 acetyl-CoA wild-type, pH 7.5, 25°C Saccharomyces cerevisiae
0.11
-
 histone H3 tail peptide wild-type, pH 7.5, 25°C Saccharomyces cerevisiae
0.62
-
 histone H3 wild-type, pH 7.5, 25°C Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.025
-
 acetyl-CoA mutant D287A/D288A, pH 7.5, 25°C Saccharomyces cerevisiae
0.025
-
 histone H3 tail peptide mutant D287A/D288A, pH 7.5, 25°C Saccharomyces cerevisiae
0.038
-
 histone H3 tail peptide mutant D288N, pH 7.5, 25°C Saccharomyces cerevisiae
0.14
-
 histone H3 tail peptide mutant D287N, pH 7.5, 25°C Saccharomyces cerevisiae
0.6
-
 acetyl-CoA mutant D288N, pH 7.5, 25°C Saccharomyces cerevisiae
0.98
-
 histone H3 tail peptide wild-type, pH 7.5, 25°C Saccharomyces cerevisiae
17
-
 acetyl-CoA mutant D287N, pH 7.5, 25°C Saccharomyces cerevisiae
90
-
 histone H3 wild-type, pH 7.5, 25°C Saccharomyces cerevisiae
390
-
 acetyl-CoA wild-type, pH 7.5, 25°C Saccharomyces cerevisiae