Any feedback?
Information on EC 6.2.1.1 - acetate-CoA ligase and Organism(s) Mus musculus and UniProt Accession Q99NB1
for references in articles please use BRENDA:EC6.2.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
6.2.1.1 acetate-CoA ligaseIUBMB Comments
Also acts on propanoate and propenoate.
Specify your search results
Word Map
- 6.2.1.1
- synthetases
- peroxisomal
- palmitate
- acyltransferase
- cholesterol
- phospholipid
- triglyceride
-
beta-oxidation
- citrate
-
arachidonic
- carnitine
-
medium-chain
- triacylglycerols
- triacsin
- palmitoyl-coa
-
oleic
-
lipogenesis
- glyoxylate
-
6.2.1.3
- oleate
-
acsls
-
hypolipidemic
-
codhs
-
acetogenic
- propionyl-coa
- fadd
- phosphotransacetylase
-
wood-ljungdahl
-
atp-citrate
- oleoyl-coa
-
glucose-limited
-
arachnoid
- sn-glycerol-3-phosphate
- coash
-
moorella
-
1-14cacetate
- corrinoid
-
fatps
- thermoaceticum
- arachidonoyl-coa
- acetoacetyl-coa
-
very-long-chain
- adrenoleukodystrophy
-
reacylation
-
vlcfas
-
extradural
- butyryl-coa
-
alpha2beta2
- myristoyl-coa
- acaca
- medicine
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
acyl-coa synthetase, acetyl-coa synthetase, acss2, acetyl-coa synthase, acetyl coa synthetase, acetyl-coenzyme a synthetase, codh/acs, acecs2, acetyl coenzyme a synthetase, acecs1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AceCS
-
-
-
-
AceCS1
Acetate thiokinase
-
-
-
-
Acetate--CoA ligase
-
-
-
-
Acetic thiokinase
-
-
-
-
Acetyl activating enzyme
-
-
-
-
Acetyl CoA ligase
-
-
-
-
Acetyl CoA synthase
-
-
-
-
Acetyl coenzyme A synthetase
-
-
-
-
Acetyl-CoA synthase
-
-
-
-
Acetyl-CoA synthetase
Acetyl-coenzyme A synthase
-
-
-
-
ACS
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Short chain fatty acyl-CoA synthetase
-
-
-
-
Short-chain acyl-coenzyme A synthetase
-
-
-
-
Synthetase, acetyl coenzyme A
-
-
-
-
Acetyl-CoA synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acetate:CoA ligase (AMP-forming)
Also acts on propanoate and propenoate.
CAS REGISTRY NUMBER
COMMENTARY
9012-31-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
AceCS2 plays a role in the production of energy under ketogenic conditions, such as starvation and diabetes. Acetyl-CoAs produced by AceCS2 are utilized mainly for oxidation
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
lipogenic enzyme, gene is highly induced by SREBP-1a, SREBP-1c and SREBP-2. The enzyme might also play an important role in basic cellular energy metabolism
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dATP + acetate + CoA
dAMP + diphosphate + acetyl-CoA
AceCS2 plays a role in the production of energy under ketogenic conditions, such as starvation and diabetes. Acetyl-CoAs produced by AceCS2 are utilized mainly for oxidation
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
-
lipogenic enzyme, gene is highly induced by SREBP-1a, SREBP-1c and SREBP-2. The enzyme might also play an important role in basic cellular energy metabolism
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SIRT1
-
AceCS1 is completely inactivated upon acetylation and is rapidly reactivated by SIRT3 deacetylation
-
SIRT3
-
AceCS2 is completely inactivated upon acetylation and is rapidly reactivated by SIRT3 deacetylation
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
marked induction of AceCS1 mRNA and protein during differentiation of 3T3-L1 cells, neither AceCS2 mRNA nor protein is detected in undifferentiated or differentiated 3T3-L1 cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
additional information
additional information
-
no AceCS2 activity is detected in liver. Marked induction of AceCS1 mRNA and protein during differentiation of 3T3-L1 cells, neither AceCS2 mRNA nor protein is detected in undifferentiated or differentiated 3T3-L1 cells
additional information
no AceCS2 activity is detected in liver. Marked induction of AceCS1 mRNA and protein during differentiation of 3T3-L1 cells, neither AceCS2 mRNA nor protein is detected in undifferentiated or differentiated 3T3-L1 cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
in adult mice, attenuation of hippocampal isoform ACSS2 expression impairs long-term spatial memory
physiological function
physiological function
-
tumor cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
physiological function
-
the enzyme regulates histone acetylation and hippocampal memory
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACS2L_MOUSE
682
0
74623
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the putative mitochondrial targeting signal is cleaved during the transportation of the enzyme into the mitochondria matrix
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
cells express higher levels of cytosolic acetyl-CoA synthetase ACSS2 under hypoxia than normoxia. Knockdown of ACSS2 by RNA interference in tumor cells enhances tumor cell death under long-term hypoxia in vitro. The ACSS2 suppression slows tumor growth in vivo. Tumor cells excrete acetate and the quantity increases under hypoxia, the pattern of acetate excretion follows the expression pattern of ACSS2. The ACSS2 knockdown leads to a corresponding reduction in the acetate excretion in tumor cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sone, H.; Shimano, H.; Sakakura, Y.; Inoue, N.; Amemiya-Kudo, M.; Yahagi, N.; Osawa, M.; Suzuki, H.; Yokoo, T.; Takahashi, A.; Iida, K.; Toyoshima, H.; Iwama, A.; Yamada, N.
Acetyl-coenzyme A synthetase is a lipogenic enzyme controlled by SREBP-1 and energy status
Am. J. Physiol.
282
E222-E230
2002
Mus musculus
Fujino, T.; Kondo, J.; Ishikawa, M.; Morikawa, K.; Yamamoto, T.T.
Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
J. Biol. Chem.
276
11420-11426
2001
Mus musculus, Mus musculus (Q99NB1), Bos taurus (Q9BEA3), Bos taurus
Hallows, W.C.; Lee, S.; Denu, J.M.
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Proc. Natl. Acad. Sci. USA
103
10230-10235
2006
Mus musculus
Yoshii, Y.; Furukawa, T.; Yoshii, H.; Mori, T.; Kiyono, Y.; Waki, A.; Kobayashi, M.; Tsujikawa, T.; Kudo, T.; Okazawa, H.; Yonekura, Y.; Fujibayashi, Y.
Cytosolic acetyl-CoA synthetase affected tumor cell survival under hypoxia: the possible function in tumor acetyl-CoA/acetate metabolism
Cancer Sci.
100
821-827
2009
Mus musculus
EXTERNAL LINKS (specific for EC-Number 6.2.1.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
