Information on EC 2.4.2.B16 - protein-long-chain fatty-acyl-lysine deacylase (NAD+)

Word Map on EC 2.4.2.B16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
2.4.2.B16
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
protein-long-chain fatty-acyl-lysine deacylase (NAD+)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + [protein]-N6-palmitoyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
NAD+ + Ac-AK(N6-acetyl)K-7-amido-4-methylcoumarin
nicotinamide + Ac-AKK-7-amido-4-methylcoumarin + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the substrate is based on the human tumour suppressor protein p53
-
-
?
NAD+ + Ac-HK(N6-acetyl)K-7-amido-4-methylcoumarin
nicotinamide + Ac-HKK-7-amido-4-methylcoumarin + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the substrate is based on the human tumour suppressor protein p53
-
-
?
NAD+ + Ac-RHK(N6-acetyl)K-7-amido-4-methylcoumarin
nicotinamide + Ac-RHKK-7-amido-4-methylcoumarin + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the substrate is based on the amino acids 379-382 of the human tumour suppressor protein p53
-
-
?
NAD+ + Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
nicotinamide + Ac-RYQK-7-amido-4-methylcoumarin + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the peptide substrate mimics the biological deacetylation site of histone H3 K56
-
-
?
NAD+ + Ac-TAR(N6-acetyl)K-7-amido-4-methylcoumarin
nicotinamide + Ac-TARK-7-amido-4-methylcoumarin + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the peptide substrate mimics the biological deacetylation site of histone H3 K9
-
-
?
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
the enzyme shows increased reaction velocity with increasing acyl chain length. As compared to its deacetylating activity, Sir2Af2 depropionylates, debutyrylates, and demyristoylates a peptide of the same sequence at 1.5-, 1.9-, and 3.4-fold higher rates, respectively
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
show the reaction diagram
-
the enzyme shows increased reaction velocity with increasing acyl chain length. As compared to its deacetylating activity, Sir2Af2 depropionylates, debutyrylates, and demyristoylates a peptide of the same sequence at 1.5-, 1.9-, and 3.4-fold higher rates, respectively
-
-
?
NAD+ + KGLGKGGA(N6-myristoyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
the enzyme shows increased reaction velocity with increasing acyl chain length. As compared to its deacetylating activity, Sir2Af2 depropionylates, debutyrylates, and demyristoylates a peptide of the same sequence at 1.5-, 1.9-, and 3.4-fold higher rates, respectively
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
show the reaction diagram
-
the enzyme shows increased reaction velocity with increasing acyl chain length. As compared to its deacetylating activity, Sir2Af2 depropionylates, debutyrylates, and demyristoylates a peptide of the same sequence at 1.5-, 1.9-, and 3.4-fold higher rates, respectively
-
-
?
NAD+ + QTAR(N6-decanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + QTAR(N6-dodecanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-dodecanoyl-ADP-ribose
show the reaction diagram
-
dodecanoylated histone H3 peptide, about 60% compared to the activity with the decanoylated peptide
-
-
?
NAD+ + QTAR(N6-hexanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-propionyl-ADP-ribose
show the reaction diagram
-
hexanoylated histone H3 peptide, about 20% compared to the activity with the decanoylated peptide
-
-
?
NAD+ + QTAR(N6-myristoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-decanoyl-ADP-ribose
show the reaction diagram
-
myristoylated histone H3 peptide, about 60% compared to the activity with the decanoylated peptide
-
-
?
NAD+ + QTAR(N6-octanoyl)KSTGG
nicotinamide + QTARKSTGG + 2'-O-octanoyl-ADP-ribose
show the reaction diagram
-
octanoylated histone H3 peptide, about 50% compared to the activity with the decanoylated peptide
-
-
?
NAD+ + SKEYFS(N6-acetyl)KQK
nicotinamide + SKEYFSKQK + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone 3]-N6-acetyl-L-lysine9
nicotinamide + [histone 3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone 3]-N6-palmitoyl-L-lysine
nicotinamide + [histone 3]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3 peptide]-N6-acetyl-L-lysine
nicotinamide + [histone H3 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H3 peptide]-N6-butyryl-L-lysine
nicotinamide + [histone H3 peptide]-L-lysine + 2'-O-butyryl-ADP-ribose
show the reaction diagram
NAD+ + [histone H3 peptide]-N6-myristoyl-L-lysine
nicotinamide + [histone H3 peptide]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H3 peptide]-N6-octanoyl-L-lysine
nicotinamide + [histone H3 peptide]-L-lysine + 2'-O-octanoyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H3 peptide]-N6-palmitoyl-L-lysine
nicotinamide + [histone H3 peptide]-L-lysine + 2'-O-palmitoyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [histone H3]-N6-acetyl-L-lysine18
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine56
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine9
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
NAD+ + [histone H3]-N6-myristoyl-L-lysine
nicotinamide + [histone H3]-L-lysine + 2'-O-myristoyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-palmitoyl-L-lysine
nicotinamide + [histone H3]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-palmitoyl-L-lysine9
nicotinamide + [histone H3]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine
nicotinamide + [histone H4]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
NAD+ + [protein]-N6-palmitoyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
NAD+ + [synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine19
nicotinamide + [synthetic tumor necrosis factor alpha peptide]-L-lysine19 + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine20
nicotinamide + [synthetic tumor necrosis factor alpha peptide]-L-lysine20 + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [tumor necrosis factor alpha]-N6-acyl-L-lysine20
nicotinamide + [tumor necrosis factor alpha]-L-lysine20 + 2'-O-acyl-ADP-ribose
show the reaction diagram
-
SIRT6 promotes the secretion of tumor necrosis factor alpha by removing the fatty acyl modification on K19 and K20 of TNFalpha
-
-
?
NAD+ + [tumor necrosis factor alpha]-N6-myristoyl-L-lysine
nicotinamide + [tumor necrosis factor alpha]-L-lysine + 2'-O-myristoyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [tumor necrosis factor-alpha]-N6-acetyl-L-lysine9
nicotinamide + [tumor necrosis factor-alpha]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
NAD+ + [histone 3]-N6-palmitoyl-L-lysine
nicotinamide + [histone 3]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine18
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine56
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H3]-N6-acetyl-L-lysine9
nicotinamide + [histone H3]-L-lysine + 2'-O-acetyl-ADP ribose
show the reaction diagram
NAD+ + [histone H3]-N6-palmitoyl-L-lysine9
nicotinamide + [histone H3]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [histone H4]-N6-acetyl-L-lysine
nicotinamide + [histone H4]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
-
?
NAD+ + [protein]-N6-palmitoyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-palmitoyl-ADP ribose
show the reaction diagram
NAD+ + [tumor necrosis factor alpha]-N6-acyl-L-lysine20
nicotinamide + [tumor necrosis factor alpha]-L-lysine20 + 2'-O-acyl-ADP-ribose
show the reaction diagram
-
SIRT6 promotes the secretion of tumor necrosis factor alpha by removing the fatty acyl modification on K19 and K20 of TNFalpha
-
-
?
additional information
?
-
-
the enzyme preferentially hydrolyzes long-chain fatty acyl groups over acetyl groups in vitro
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4R)-1-[(benzyloxy)carbonyl]-4-hydroxy-L-prolyl-N6-ethanethioyl-N-phenyl-L-lysinamide
-
0.2 mM, 56% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
1-(tert-butoxycarbonyl)-L-prolyl-N6-ethanethioyl-N-phenyl-L-lysinamide
-
0.2 mM, 32% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
3-morpholinosydnonimine
-
-
6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide
-
i.e. EX-527. 0.2 mM, 56% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
H2N-AK-(Nepsilon-thioacetyl-lysine)-LM-COOH
-
moderate potent inhibitor
-
H2N-HK-(Nepsilon-thioacetyllysine)-LM-COOH
-
moderate potent inhibitor
-
luteolin
-
30% inhibition at 0.1 mM
methyl N2-acetyl-N6-ethanethioyl-L-lysyl-L-alaninate
-
0.2 mM, 20% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
N2-[(benzyloxy)carbonyl]-N6-ethanethioyl-N-(2-fluorophenyl)-L-lysinamide
-
0.2 mM, 25% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
N2-[(benzyloxy)carbonyl]-N6-ethanethioyl-N-pyridin-3-yl-L-lysinamide
-
0.2 mM, 54% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
N2-[(benzyloxy)carbonyl]-N6-ethanethioyl-N-[2-(4-methoxyphenyl)-2-oxoethyl]-L-lysinamide
-
0.2 mM, 48% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amino-4-methylcoumarin
N6-ethanethioyl-N-(2-oxo-2-phenylethyl)-N2-(3-phenylpropanoyl)-L-lysinamide
-
0.2 mM, 20% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
N6-ethanethioyl-N-phenyl-N2-[3-(pyridin-3-yl)propanoyl]-L-lysinamide
-
0.2 mM, 18% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
N6-ethanethioyl-N2-(3-phenylpropanoyl)-L-lysyl-L-alanine
-
0.2 mM, 20% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amido-4-methylcoumarin
N6-ethanethioyl-N2-[3-(2-fluorophenyl)propanoyl]-N-pyridin-3-yl-L-lysinamide
-
0.2 mM, 58% inhibition, substrate: Ac-RYQ(N6-acetyl)K-7-amino-4-methylcoumarin
nicotinamide
-
inhibits the deacetylation of native histones much more effectively than deacetylation of a synthetic substrate
quercetin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
linoleic acid
-
EC50 value of 0.089 mM
luteolin
-
EC50 value of 0.27 mM
N-(alpha-linolenoyl)ethanolamine
-
-
-
N-(gama-linolenoyl)ethanolamine
-
-
-
N-linoleoylethanolamine
-
-
-
N-myristoylethanolamine
-
; EC50 value of 0.0075 mM
N-oleoylethanolamine
-
strongest activator with EC50 value of 0.0031 mM
N-palmitoleoylethanolamine
-
-
-
N-palmitoylethanolamine
-
-
oleic acid
-
EC50 value of 0.23 mM
quercetin
-
EC50 value of 0.99 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
SKEYFS(N6-acetyl)KQK
-
pH 7.8, 37°C
-
0.232
[histone 3]-N6-acetyl-L-lysine9
-
at pH 8.0 and 37°C
-
0.039 - 0.81
[histone H3 peptide]-N6-acetyl-L-lysine
-
0.008 - 0.2
[histone H3 peptide]-N6-butyryl-L-lysine
-
0.0034
[histone H3 peptide]-N6-myristoyl-L-lysine
-
pH 8.0, 37°C
-
0.0012 - 0.04
[histone H3 peptide]-N6-octanoyl-L-lysine
-
0.0009
[histone H3 peptide]-N6-palmitoyl-L-lysine
-
pH 8.0, 37°C
-
0.0024
[synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine19
-
pH 8.0, 37°C
-
0.0045
[synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine20
-
pH 8.0, 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.0039
[histone H3 peptide]-N6-acetyl-L-lysine
-
0.001 - 0.0021
[histone H3 peptide]-N6-butyryl-L-lysine
-
0.0049 - 0.01
[histone H3 peptide]-N6-myristoyl-L-lysine
-
0.001 - 0.0046
[histone H3 peptide]-N6-octanoyl-L-lysine
-
0.0027
[histone H3 peptide]-N6-palmitoyl-L-lysine
Homo sapiens
-
pH 8.0, 37°C
-
0.002
[synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine19
Homo sapiens
-
pH 8.0, 37°C
-
0.005
[synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine20
Homo sapiens
-
pH 8.0, 37°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.132
SKEYFS(N6-acetyl)KQK
Archaeoglobus fulgidus
-
pH 7.8, 37°C
197658
0.0048 - 0.026
[histone H3 peptide]-N6-acetyl-L-lysine
197651
0.01 - 0.16
[histone H3 peptide]-N6-butyryl-L-lysine
197652
0.14 - 10
[histone H3 peptide]-N6-myristoyl-L-lysine
197654
0.12 - 0.92
[histone H3 peptide]-N6-octanoyl-L-lysine
197653
3
[histone H3 peptide]-N6-palmitoyl-L-lysine
Homo sapiens
-
pH 8.0, 37°C
197655
0.83
[synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine19
Homo sapiens
-
pH 8.0, 37°C
197656
1.1
[synthetic tumor necrosis factor alpha peptide]-N6-myristoyl-L-lysine20
Homo sapiens
-
pH 8.0, 37°C
197657
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0041
luteolin
Homo sapiens
-
at pH 8.0 and 37°C
0.024
quercetin
Homo sapiens
-
at pH 8.0 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
muscle invasive urothelial carcinoma of the bladder. Decline of SIRT6 expression when bladder cancer progresses from stage T2 to stage T4
Manually annotated by BRENDA team
-
SIRT6 is down-regulated in human glioma tissues
Manually annotated by BRENDA team
-
epidermal
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
SIRT6 is highly expressed in the retina, controlling levels of histone H3K9 and H3K56 acetylation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
SIRT6 translocates into the cytoplasm under stress and regulates formation as well as disassembly of stress granules
Manually annotated by BRENDA team
-
Sirt6 partially colocalizes with mitotic spindles
Manually annotated by BRENDA team
-
Sirt6 is enriched in the nucleolus in the G1 phase of the cell cycle, while S phase nucleoli are almost entirely free of Sirt6
Manually annotated by BRENDA team
-
SIRT6 activity is nucleosome dependent, and suggest that its binding to the nucleosome might convert it into an active structure
Manually annotated by BRENDA team
-
during interphase, Sirt6 is mostly localized to the nucleus
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrosylation
-
tyrosine 257 in sirtuin 6 is nitrated after 3-morpholinosydnonimine treatment
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown by hanging drop method, structures of the enzyme bound to nictotinamide are determined from a single crystal diffracting to 2.4 A resolution. The structures show that free nicotinamide binds in a conserved pocket that participates in NAD+ binding and catalysis
-
vapor diffusion at 20°C, crystal structure of the enzyme bound to KGLGKGGA(N6-myristoyl)KRHRKW
-
hanging drop vapor diffusion at 20°C. Crystal structures in complex with ADP-ribose and the non-hydrolyzable analog of O-acetyl-ADP-ribose, 2'-N-acetyl-ADP-ribose
-
hanging drop vapor diffusion method at 18°C, crystal structure of Sirt6 in complex with a histone H3 K9 myristoyl peptide and ADPribose at 2.2 A resolution
-
hanging drop vapor diffusion method, cocrystal of enzyme with [histone H3 peptide]-N6-myristoyl-L-lysine
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione agarose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) and NIH-3T3 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli with a C-terminal His6 tag and an N-terminal T7 tag
-
expressed in HEK-293 cells
-
expressed in HEK-293T cells
-
expression in Escherichia coli
SIRT6 overexpression in terminally differentiated cortical and hippocampal neurons, mediated by a neuron-specific recombinant adeno-associated virus, downregulates cell viability under oxidative stress condition
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decline of SIRT6 expression when bladder cancer progresses from stage T2 to stage T4
-
during mitosis, the Sirt6 expression level is increased
-
enzyme expression in HCC cells is upregulated by transforming growth factor-beta1, H2O2, and HOCl
-
enzyme expression is significantly reduced in human ovarian cancer tissues compared to the normal tissues
-
H2O2 treatment significantly reduces Sirt6 protein. Stress-induced downregulation of Sirt6 is likely involved in the pathogenesis of diabetic retinopathy
-
in cortical and hippocampal neurons SIRT6 is downregulated during maturation in vitro, reaching the lowest expression at 11 days in vitro
-
SIRT6 expression is upregulated under pathologic conditions in angiotensin II-stimulated cardiac fibroblasts and in myocardium of rat subjected to abdominal aortic constriction surgery
SIRT6 is down-regulated in human glioma tissues
-
SIRT6 is upregulated in squamous cell carcinoma
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M70R
-
further decrease in nicotinamide sensitivity compared to wild-type
G60A
-
the mutant is a lysine defatty acylase in vitro with substantially decreased deacetylase activity in vitro and no detectable deacetylase activity in cells
H131Y
-
the mutant enzyme can still bind NAD+ but has a decreased ability to bind ADP-ribose
R65A
-
the mutant shows only ADP-ribosyltransferase activity but no deacetylase activity
S56Y
-
inactive
Y12F
-
the mutant exhibits deacetylase activity similar to that of the wild type enzyme
Y148F
-
the mutant shows 57% decrease of activity compared to the wild type enzyme
Y257F
-
the mutant shows 73% decrease of activity compared to the wild type enzyme
Y5F
-
the mutant exhibits deacetylase activity similar to that of the wild type enzyme
G60A
-
inactive
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine