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Literature summary extracted from

  • Brent, M.M.; Iwata, A.; Carten, J.; Zhao, K.; Marmorstein, R.
    Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus (2009), J. Biol. Chem., 284, 19412-19419.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.B27 expression in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.B27 crystals of enzyme/CoA complex are grown by hanging drop vapor diffusion in 20 days at 20°C using a well solution containing 0.1 M MES, pH 6.5, and 12% PEG 20,000. Crystals are cryoprotected using well solution supplemented with 30% glycerol Saccharolobus solfataricus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.B27 D29A reduction in activity by about 2fold Saccharolobus solfataricus
2.3.1.B27 D53N modest reduction in activity Saccharolobus solfataricus
2.3.1.B27 E42Q modest reduction in activity Saccharolobus solfataricus
2.3.1.B27 E43Q modest reduction in activity Saccharolobus solfataricus
2.3.1.B27 E76A activity is reduced to near background levels Saccharolobus solfataricus
2.3.1.B27 E76Q mutation has no effect on activity Saccharolobus solfataricus
2.3.1.B27 H36A mutant shows activity similar to the wild type enzyme Saccharolobus solfataricus
2.3.1.B27 H72A lowered activity Saccharolobus solfataricus
2.3.1.B27 H72A modest reduction in activity Saccharolobus solfataricus
2.3.1.B27 H72A/E76Q activity is reduced to near background levels Saccharolobus solfataricus
2.3.1.B27 M121H mutation results in about a 2fold increase in protein substrate Km and about a 5fold decrease in overall kcat, despite little change in the Km for acetyl-CoA Saccharolobus solfataricus
2.3.1.B27 M121Y mutation results in about a 2fold increase in protein substrate Km and about a 5fold decrease in overall kcat, despite little change in the Km for acetyl-CoA Saccharolobus solfataricus
2.3.1.B27 R33A reduction in activity to near background levels. Km for Ac-CoA is similar to wild type and elevated by about 2fold for protein substrate, whereas the overall kcat is reduced about 5fold relative to the wild type protein Saccharolobus solfataricus
2.3.1.B27 S78A the activity for both mutants is close to wild type Saccharolobus solfataricus
2.3.1.B27 S78C the activity for both mutants is close to wild type Saccharolobus solfataricus
2.3.1.B27 Y38S modest reduction in activity Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.B27 additional information
-
 [DNA-binding protein Alba1]-L-lysine16 P6A, P8A, and G15A mutants of ALBA have Km values similar to wild type ALBA, thus revealing that these residues do not play a significant role of PAT acetylation of ALBA Saccharolobus solfataricus
2.3.1.B27 0.037
-
 acetyl-CoA pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme R33A Saccharolobus solfataricus
2.3.1.B27 0.039
-
 acetyl-CoA pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme H72A/E76Q Saccharolobus solfataricus
2.3.1.B27 0.048
-
 acetyl-CoA pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121H Saccharolobus solfataricus
2.3.1.B27 0.048
-
 acetyl-CoA pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus
2.3.1.B27 0.05
-
 acetyl-CoA pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121Y Saccharolobus solfataricus
2.3.1.B27 0.059
-
 acetyl-CoA pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme E76A Saccharolobus solfataricus
2.3.1.B27 0.11
-
 [DNA-binding protein Alba1]-L-lysine16 pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus
2.3.1.B27 0.58
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus
2.3.1.B27 0.91
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme H72A/E76Q Saccharolobus solfataricus
2.3.1.B27 0.94
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme E76A Saccharolobus solfataricus
2.3.1.B27 1.2
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121H Saccharolobus solfataricus
2.3.1.B27 1.2
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme R33A Saccharolobus solfataricus
2.3.1.B27 1.3
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121Y Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.B27 acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 Saccharolobus solfataricus the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
-
 ?
2.3.1.B27 acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 Saccharolobus solfataricus P2 the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.B27 Saccharolobus solfataricus Q97V23
-
-
2.3.1.B27 Saccharolobus solfataricus P2 Q97V23
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.B27
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.B27 acetyl-CoA + VLIGKKPVMNY
-
 Saccharolobus solfataricus CoA + VLIG-K(Ac)-KPVMNY
-
 ?
2.3.1.B27 acetyl-CoA + VLIGKKPVMNY
-
 Saccharolobus solfataricus P2 CoA + VLIG-K(Ac)-KPVMNY
-
 ?
2.3.1.B27 acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
-
 Saccharolobus solfataricus CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
-
 ?
2.3.1.B27 acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes Saccharolobus solfataricus CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
-
 ?
2.3.1.B27 acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
-
 Saccharolobus solfataricus P2 CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
-
 ?
2.3.1.B27 acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes Saccharolobus solfataricus P2 CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.B27 75
-
 assay at Saccharolobus solfataricus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.1.B27 additional information
-
 the enzyme is nearly completely inactive at room temperature Saccharolobus solfataricus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.B27 0.0067
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme E76A Saccharolobus solfataricus
2.3.1.B27 0.0067
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121Y Saccharolobus solfataricus
2.3.1.B27 0.0083
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme R33A Saccharolobus solfataricus
2.3.1.B27 0.0092
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121H Saccharolobus solfataricus
2.3.1.B27 0.022
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme H72A/E76Q Saccharolobus solfataricus
2.3.1.B27 0.0385
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus
2.3.1.B27 0.0385
-
 [DNA-binding protein Alba1]-L-lysine16 pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.B27 8
-
 assay at Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
2.3.1.B27 physiological function the Sulfolobus solfataricus protein acetyltransferase acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys16 to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a primitive model for chromatin regulation analogous to histone modification in eukaryotes Saccharolobus solfataricus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.B27 0.0051
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121Y Saccharolobus solfataricus
2.3.1.B27 0.0069
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme R33A Saccharolobus solfataricus
2.3.1.B27 0.0071
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme E76A Saccharolobus solfataricus
2.3.1.B27 0.0077
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme M121H Saccharolobus solfataricus
2.3.1.B27 0.024
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, mutant enzyme H72A/E76Q Saccharolobus solfataricus
2.3.1.B27 0.066
-
 VLIGKKPVMNY pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus
2.3.1.B27 0.35
-
 [DNA-binding protein Alba1]-L-lysine16 pH 8.0, 75°C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme Saccharolobus solfataricus