Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.32 extracted from

  • Berndsen, C.E.; Denu, J.M.
    Catalysis and substrate selection by histone/protein lysine acetyltransferases (2008), Curr. Opin. Struct. Biol., 18, 682-689.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
histone chaperone Rtt109 associates with chaperone Vps75 (H3K9 and H3K23 acetylation in vivo) or Asf1 (H3K56 acetylation in vivo), stimulation of catalytic activity by chaperones, R55109 stimulates histone deposition by the chaperones, the complex of enzyme + chaperone alters substrate specificity, targets to specific loci, enhances acetyltransferase activity, restricts access of non-target proteins, and coordinates the multiple enzyme activities of the complex Saccharomyces cerevisiae
piccolo NuA4 complex accessory proteins to support the function of Esa1, stimulating the catalytic activity of the enzyme Saccharomyces cerevisiae
SAGA complex histone ubiquitin protease Ubp8 and histone acetyltransferase Gcn5 form a complex Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0003
-
acetyl-CoA Rtt109 Saccharomyces cerevisiae
0.001
-
acetyl-CoA Esa1 Saccharomyces cerevisiae
0.001
-
acetyl-CoA Rtt109 in complex with chaperone Vps75 Saccharomyces cerevisiae
0.0025
-
acetyl-CoA Gcn5 Saccharomyces cerevisiae
0.0025
-
acetyl-CoA Esa1 in piccolo NuA4-complex with Yng2 and Epl1 Saccharomyces cerevisiae
0.04
-
acetyl-CoA p300 Saccharomyces cerevisiae
0.075
-
histone Rtt109 in complex with chaperone Vps75 Saccharomyces cerevisiae
0.083
-
histone Rtt109 Saccharomyces cerevisiae
0.16
-
histone p300 Saccharomyces cerevisiae
0.22
-
histone Esa1 in piccolo NuA4-complex with Yng2 and Epl1 Saccharomyces cerevisiae
0.49
-
histone Gcn5 Saccharomyces cerevisiae
1.4
-
histone Esa1 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + histone Homo sapiens
-
CoA + acetyl-histone
-
?
acetyl-CoA + histone Saccharomyces cerevisiae
-
CoA + acetyl-histone
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae
-
?
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + histone
-
Homo sapiens CoA + acetyl-histone
-
?
acetyl-CoA + histone
-
Saccharomyces cerevisiae CoA + acetyl-histone
-
?
acetyl-CoA + histone peptide
-
Saccharomyces cerevisiae CoA + acetylated histone peptide
-
r

Synonyms

Synonyms Comment Organism
Esa1 histone target lysine H4K5, K8, K12, Htz1K14, minimum complex formation is necessary to exhibit full catalytic activity and for nucleosome recognition Saccharomyces cerevisiae
Gcn5 histone target lysine H3K9, 14, 36, constitutively active, can form a SAGA complex with histone ubiquitin protease Ubp8 Saccharomyces cerevisiae
HAT
-
Homo sapiens
HAT
-
Saccharomyces cerevisiae
histone/protein lysine acetyltransferase
-
Homo sapiens
histone/protein lysine acetyltransferase
-
Saccharomyces cerevisiae
p/CAF human histone target lysine H3K14, constitutively active Homo sapiens
p300 histone target lysine H2AK5, H2B, constitutively active, broad protein specificity Saccharomyces cerevisiae
Rtt109 histone acetyltransferase histone target lysine H3K56, K9, K23, complex formation necessary to exhibit full catalytic activity Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0017
-
histone Rtt109 Saccharomyces cerevisiae
0.0019
-
histone Esa1 Saccharomyces cerevisiae
0.13
-
histone Rtt109 in complex with chaperone Vps75 Saccharomyces cerevisiae
1.6
-
histone Esa1 in piccolo NuA4-complex Saccharomyces cerevisiae
1.7
-
histone Gcn5 Saccharomyces cerevisiae
4.1
-
histone peptide p300 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function transcriptional regulation via histone complex acetylation, possibility of longer chain acyl-CoA transfers is proposed for histone acetyltransferases Homo sapiens
physiological function transcriptional regulation via histone complex acetylation, possibility of longer chain acyl-CoA transfers is proposed for histone acetyltransferases Saccharomyces cerevisiae