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Information on EC 2.3.1.B41 - protein-long-chain fatty-acyl-lysine deacylase (NAD+) and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30124

for references in articles please use BRENDA:EC2.3.1.B41
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Archaeoglobus fulgidus
UNIPROT: O30124
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Synonyms
sirt6, deacylase, sirtuin 6, adp-ribosyl transferase, nad+-dependent histone deacetylase, nicotinamide adenine dinucleotide-dependent deacetylase, sirtuin-6, sirtuin6, sirt6 deacetylase, histone deacetylase sirtuin 6, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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+ + SKEYFS(N6-acetyl)KQK
nicotinamide + SKEYFSKQK + 2'-O-acetyl-ADP-ribose
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
nicotinamide insensitivity, IC50: 2.1 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
SKEYFS(N6-acetyl)KQK
pH 7.8, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.132
SKEYFS(N6-acetyl)KQK
pH 7.8, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M70R
further decrease in nicotinamide sensitivity compared to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Avalos, J.L.; Bever, K.M.; Wolberger, C.
Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
Mol. Cell
17
855-868
2005
Archaeoglobus fulgidus (O30124)
Manually annotated by BRENDA team
Fischer, F.; Gertz, M.; Suenkel, B.; Lakshminarasimhan, M.; Schutkowski, M.; Steegborn, C.
Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition
PLoS One
7
e45098
2012
Archaeoglobus fulgidus (O30124)
Manually annotated by BRENDA team
Ringel, A.E.; Roman, C.; Wolberger, C.
Alternate deacylating specificities of the archaeal sirtuins Sir2Af1 and Sir2Af2
Protein Sci.
23
1686-1697
2014
Archaeoglobus fulgidus (O30124)
Manually annotated by BRENDA team