Information on EC 2.3.1.B27 - protein acetyltransferase (Alba1-protein acetylating)

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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus

EC NUMBER
COMMENTARY hide
2.3.1.B27
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
protein acetyltransferase (Alba1-protein acetylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16 = CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[DNA-binding protein Alba1]-L-lysine N6-acetyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + VLIGKKPVMNY
CoA + VLIG-K(Ac)-KPVMNY
show the reaction diagram
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [DNA-binding protein Alba1]-L-lysine16
CoA + [DNA-binding protein Alba1]-N6-acetyl-L-lysine16
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 0.059
acetyl-CoA
0.58 - 1.3
VLIGKKPVMNY
0.11
[DNA-binding protein Alba1]-L-lysine16
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pH 8.0, 75C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme
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additional information
[DNA-binding protein Alba1]-L-lysine16
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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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067 - 0.0385
VLIGKKPVMNY
0.0385
[DNA-binding protein Alba1]-L-lysine16
Sulfolobus solfataricus
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pH 8.0, 75C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0051 - 0.066
VLIGKKPVMNY
5881
0.35
[DNA-binding protein Alba1]-L-lysine16
Sulfolobus solfataricus
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pH 8.0, 75C, ALBA 11-mer peptide with the sequence VLIGKKPVMNY, wild-type enzyme
19789
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme is nearly completely inactive at room temperature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19667
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1 * 19667, mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of enzyme/CoA complex are grown by hanging drop vapor diffusion in 20 days at 20C 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
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sitting-drop vapour-diffusion technique, 1.7 A resolution, the crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.30, b = 46.59, c = 68.39 A
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a C-terminally hexahistidine-tagged protein
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expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D29A
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reduction in activity by about 2fold
D53N
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modest reduction in activity
E42Q
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modest reduction in activity
E43Q
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modest reduction in activity
E76A
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activity is reduced to near background levels
E76Q
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mutation has no effect on activity
H36A
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mutant shows activity similar to the wild type enzyme
H72A
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lowered activity; modest reduction in activity
H72A/E76Q
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activity is reduced to near background levels
M121H
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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
M121Y
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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
R33A
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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
S78A
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the activity for both mutants is close to wild type
S78C
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the activity for both mutants is close to wild type
Y38S
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modest reduction in activity
D29A
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reduction in activity by about 2fold
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E42Q
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modest reduction in activity
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E76Q
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mutation has no effect on activity
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H36A
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mutant shows activity similar to the wild type enzyme
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R33A
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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
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