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Information on EC 2.3.1.B44 - actin N-acetyltransferase and Organism(s) Homo sapiens and UniProt Accession Q93015

for references in articles please use BRENDA:EC2.3.1.B44
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.B44 actin N-acetyltransferase
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q93015 not found.
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Word Map
  • 2.3.1.B44
  • nt-acetylation
  • cytoskeletal
  • actin-binding
  • profilins
  • posttranslationally
  • depolymerization
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Homo sapiens
Reaction Schemes
+
an actin N-terminus
=
a N-acetylactin
+
Synonyms
naa80, n-alpha-acetyltransferase 80, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-alpha-acetyltransferase 80
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:actin N-acetyltransferase
-
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 + actin
CoA + N-acetyl-actin
show the reaction diagram
-
-
-
?
acetyl-CoA + CDEDETT
CoA + N-acetyl-CDEDETT
show the reaction diagram
peptide dervied from alpha-actin 1 N-terminus
-
-
?
acetyl-CoA + CEEEDST
CoA + N-acetyl-CEEEDST
show the reaction diagram
best substrate
-
-
?
acetyl-CoA + DDDI24
CoA + N-acetyl-DDDI24
show the reaction diagram
-
-
-
?
acetyl-CoA + DDDIAA
CoA + N-acetyl-DDDIAA
show the reaction diagram
peptide dervied from beta-actin N-terminus
-
-
?
acetyl-CoA + EEEI24
CoA + N-acetyl-EEEI24
show the reaction diagram
-
-
-
?
acetyl-CoA + MCDEDET
CoA + N-acetyl-MCDEDET
show the reaction diagram
peptide dervied from alpha-actin 1 N-terminus
-
-
?
acetyl-CoA + MCEEEDS
CoA + N-acetyl-MCEEEDS
show the reaction diagram
-
-
-
?
acetyl-CoA + MDDD24
CoA + N-acetyl-MDDD24
show the reaction diagram
-
-
-
?
acetyl-CoA + MDDDIAA
CoA + N-acetyl-MDDDIAA
show the reaction diagram
peptide dervied from beta-actin N-terminus
-
-
?
acetyl-CoA + MDEL24
CoA + N-acetyl-MDEL24
show the reaction diagram
-
-
-
?
acetyl-CoA + MEEEIAA
CoA + N-acetyl-MEEEIAA
show the reaction diagram
peptide dervied from gamma-actin 1 N-terminus
-
-
?
acetyl-CoA + nuclear import factor Rch1 residues 23-82
CoA + N-acetyl-nuclear import factor Rch1 residues 23-82
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A-acetyl-DDDI-NH2
-
coenzyme A-acetyl-EEEI-NH2
-
coenzyme A-acetyl-MDEL-NH2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0505
DDDI24
pH not specified in the publication, temperature not specified in the publication
-
0.4
DDDIAA
pH 7.5, 30°C
0.0424
EEEI24
pH not specified in the publication, temperature not specified in the publication
-
0.5
MDDDIAA
pH 7.5, 30°C
0.119
MDEL24
pH not specified in the publication, temperature not specified in the publication
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000043
coenzyme A-acetyl-DDDI-NH2
pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00038
coenzyme A-acetyl-DDDI-NH2
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
diffuse cytosolic distribution
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAA80_HUMAN
286
0
31445
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of NAA80 in complex with an inhibitor. NAA80 adopts a fold similar to other N-acetyltransferases but with a more open substrate binding region
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K73A
mutation corresponding to residue that interacts with D3 of substrate, reduction in activity
R43A
mutation corresponding to residue that interacts with D2 of substrate, loss of activity
S88A
mutation corresponding to residue that interacts with D3 of substrate, reduction of activity
W36A
mutation corresponding to residue that interacts with D2 of substrate, loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HAP-1 cell
expression in HAP1-cell
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wiame, E.; Tahay, G.; Tyteca, D.; Vertommen, D.; Stroobant, V.; Bommer, G.T.; Van Schaftingen, E.
NAT6 acetylates the N-terminus of different forms of actin
FEBS J.
285
3299-3316
2018
Homo sapiens (Q93015)
Manually annotated by BRENDA team
Zegerman, P.; Bannister, A.J.; Kouzarides, T.
The putative tumour suppressor Fus-2 is an N-acetyltransferase
Oncogene
19
161-163
2000
Homo sapiens (Q93015)
Manually annotated by BRENDA team
Drazic, A.; Aksnes, H.; Marie, M.; Boczkowska, M.; Varland, S.; Timmerman, E.; Foyn, H.; Glomnes, N.; Rebowski, G.; Impens, F.; Gevaert, K.; Dominguez, R.; Anesen, T.
NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility
Proc. Natl. Acad. Sci. USA
115
4399-4404
2018
Homo sapiens (Q93015)
Manually annotated by BRENDA team
Goris, M.; Magin, R.S.; Foyn, H.; Myklebust, L.M.; Varland, S.; Ree, R.; Drazic, A.; Bhambra, P.; Stoeve, S.I.; Baumann, M.; Haug, B.E.; Marmorstein, R.; Arnesen, T.
Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80
Proc. Natl. Acad. Sci. USA
115
4405-4410
2018
Homo sapiens (Q93015)
Manually annotated by BRENDA team