6.4.1.2: acetyl-CoA carboxylase
This is an abbreviated version!
For detailed information about acetyl-CoA carboxylase, go to the full flat file.
Word Map on EC 6.4.1.2
-
6.4.1.2
-
amp-activated
-
triglyceride
-
lipogenesis
-
adipose
-
lipogenic
-
sterol
-
peroxisome
-
cholesterol
-
obesity
-
carnitine
-
malonyl-coa
-
proliferator-activated
-
high-fat
-
adipocytes
-
lipoprotein
-
element-binding
-
biotin
-
steatosis
-
lipase
-
obese
-
herbicide
-
srebp-1c
-
triacylglycerols
-
diet-induced
-
stearoyl-coa
-
malic
-
adiponectin
-
nafld
-
lipolysis
-
monophosphate-activated
-
hfd-induced
-
protein-1c
-
weed
-
carboxylases
-
aicar
-
atp-citrate
-
malonyl
-
desaturase-1
-
anti-obesity
-
biotin-dependent
-
hormone-sensitive
-
chrebp
-
5'-amp-activated
-
palmitoyltransferase-1
-
target-site
-
adenoid
-
srebf1
-
anti-adipogenic
-
lolium
-
biotechnology
-
medicine
-
herbicide-resistant
-
pharmacology
-
synthesis
-
drug development
-
biofuel production
-
agriculture
- 6.4.1.2
-
amp-activated
- triglyceride
-
lipogenesis
- adipose
-
lipogenic
- sterol
- peroxisome
- cholesterol
- obesity
- carnitine
- malonyl-coa
-
proliferator-activated
-
high-fat
- adipocytes
- lipoprotein
-
element-binding
- biotin
- steatosis
- lipase
-
obese
-
herbicide
- srebp-1c
- triacylglycerols
-
diet-induced
- stearoyl-coa
-
malic
- adiponectin
- nafld
-
lipolysis
-
monophosphate-activated
-
hfd-induced
- protein-1c
-
weed
- carboxylases
- aicar
-
atp-citrate
-
malonyl
-
desaturase-1
-
anti-obesity
-
biotin-dependent
-
hormone-sensitive
-
chrebp
-
5'-amp-activated
-
palmitoyltransferase-1
-
target-site
- adenoid
-
srebf1
-
anti-adipogenic
- lolium
- biotechnology
- medicine
-
herbicide-resistant
- pharmacology
- synthesis
- drug development
- biofuel production
- agriculture
Reaction
Synonyms
ACACA, ACACB, ACC, ACC-1, ACC-2, ACC1, Acc1a, Acc1b, Acc1p, ACC2, AccA, ACCalpha, ACCase, ACCase 1, ACCB, AccC, Acetyl CoA carboxylase, Acetyl coenzyme A carboxylase, acetyl coenzyme A carboxylase alpha, acetyl-CoA carboxylase, acetyl-CoA carboxylase 1, acetyl-CoA carboxylase 2, acetyl-CoA carboxylase A, acetyl-CoA carboxylase alpha, acetyl-CoA carboxylase B, acetyl-CoA carboxylase-2, acetyl-CoA carboxylase-alpha, acetyl-CoA-carboxylase, acetyl-CoA/propionyl-CoA carboxylase, Acetyl-coenzyme A carboxylase, acetyl-coenzyme-A carboxylase, acetylCoA carboxylase, acyl coenzyme A carboxylase, acyl-CoA carboxylase, BCCP1, BCCP2, CAC1A, CAC1B, Carboxylase, acetyl coenzyme A, Hfa1p, More, PccB
ECTree
6.4.1.2 acetyl-CoA carboxylaseAdvanced search results
results (
results (Metals Ions
Metals Ions on EC 6.4.1.2 - acetyl-CoA carboxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Co2+
Cs+
K+
Mg2+
Mn2+
NH4+
phosphate
additional information
Co2+
Q877I4; Q877I3; Q877I5
26% of the maximum activity is observed when Co2+ (10 to 15 mM) is used as a divalent cation
Cs+
-
small activating effect, depends on the degree of saturation of the reaction by HCO3-
K+
-
small activating effect, depends on the degree of saturation of the reaction by HCO3-
K+
-
greatest activation at 12-15 mM K+, at HCO3- concentration of 0.18 mM, 1 mM, and 10 mM
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
optimal concentration of 9686 enzyme: 5 mM, optimal concentration of Wayne enzyme: 3 mM
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
concentration of Mg2+ must be sufficient to allow chelation by both ATP and citrate. Free Mg2+ inhibits
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
maximal activation when ATP exists largely as MgATP2- with low concentrations of free Mg2+
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
Q877I4; Q877I3; Q877I5
1.0 mM Mn2+ gives 82% of the maximum activity obtained with the Mg2+ ion
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
Mn2+ or Mg2+ essential for activity. Maximal activation at 1.5 mM Mn2+
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
maximal activity at 1 mM Mn2+ with 1 mM ATP. Maximal activity is 25% of that observed with Mg2+
phosphate
-
phosphate content of the 10000000 MW enzyme form: 4.0 mol of phosphate per mol of subunit. Phosphate content of the 2000000 MW enzyme form: 6.0 mol phosphate per mol of subunit. The 10000000 MW subunit and the 2000000 MW subunit are interconvertible by phosphorylation and dephosphorylation. Dephosphorylation by [acetyl-CoA carboxylase]-phosphatase 2 activates the enzyme and reduces its dependence on citrate
phosphate
-
contains approximately 6 mol phosphate per 240000 g of protein
additional information
Q877I4; Q877I5; Q877I3
Fe2+, Cu2+, Ca2+, and Ni2+ (0.5 to 20 mM) have no effect on enzyme activity
additional information
-
Fe2+, Cu2+, Ca2+, and Ni2+ (0.5 to 20 mM) have no effect on enzyme activity
additional information
-
the zinc domain in bacterial carboxyltransferase belongs to the zinc ribbon class of zinc fingers, Zn domains are commonly associated with DNA binding
