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EC Tree
IUBMB Comments Simultaneously dephosphorylates and activates EC 6.4.1.2 acetyl-CoA carboxylase. Acts similarly on EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase), EC 2.4.1.1 (phosphorylase), EC 2.4.1.11 [glycogen(starch) synthase], and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate. Not identical to EC 3.1.3.17 ([phosphorylase] phosphatase ) or EC 3.1.3.43 {[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase}.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acetyl-coa carboxylase phosphatase, [acetyl-coa carboxylase]-phosphatase,
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acetyl-CoA carboxylase phosphatase
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phosphatase, acetyl coenzyme A carboxylase
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protein phosphatase 2A
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[acetyl-CoA carboxylase] phosphate + H2O = [acetyl-CoA carboxylase] + phosphate
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hydrolysis of phosphoric ester
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[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase
Simultaneously dephosphorylates and activates EC 6.4.1.2 acetyl-CoA carboxylase. Acts similarly on EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase), EC 2.4.1.1 (phosphorylase), EC 2.4.1.11 [glycogen(starch) synthase], and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate. Not identical to EC 3.1.3.17 ([phosphorylase] phosphatase ) or EC 3.1.3.43 {[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase}.
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p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
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?
phosphohistone + H2O
histone + phosphate
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?
phosphoprotamine + H2O
protamine + phosphate
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?
[3-hydroxy-3-methylglutaryl-CoA reductase]-phosphate + H2O
3-hydroxy-3-methylglutaryl-CoA reductase + phosphate
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?
[acetyl-CoA carboxylase]-phosphate + H2O
acetyl-CoA carboxylase + phosphate
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?
[glycogen phosphorylase A]-phosphate
[glycogen phosphorylase A] + phosphate
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?
[glycogen-phosphorylase a]-phosphate + H2O
glycogen-phosphorylase a + phosphate
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[glycogen-synthase]-phosphate + H2O
glycogen-synthase + phosphate
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?
[phosphoralase a]-phosphate + H2O
phosphoralase a + phosphate
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[phosphorylase a]-phosphate
[phosphorylase a] + phosphate
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Mn2+
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activates
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acetyl-CoA carboxylase
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inhibits dephosphorylation of phosphoprotamine
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F-
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50 mM, no effect on dephosphorylation of [acetyl-CoA carboxylase], strong inhibition of the dephosphorylation of [phosphorylase a]-phosphate
okadaic acid
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inhibitis carboxymethylation of 36 kDa subunit of enzyme
phosphate
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strong inhibitor when phosphoprotamine or [phosphorylase a]-phosphate is the substrate, the effect is far less apparent when [acetyl-CoA carboxylase]-phosphate is used as the substrate
additional information
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no inhibition by the rat liver phosphorylase phosphatase inhibitor protein
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Mg2+
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activation of carboxymethylation of 36 kDa subunit of enzyme
additional information
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not activating carboxymethylation: glutamate
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1.34
p-nitrophenyl phosphate
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0.02
phosphohistone
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0.076
phosphoprotamine
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0.0002 - 0.0015
[acetyl-CoA carboxylase]-phosphate
0.037
[glycogen phosphorylase A]-phosphate
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0.0055
[phosphorylase a]-phosphate
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0.0002
[acetyl-CoA carboxylase]-phosphate
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0.0015
[acetyl-CoA carboxylase]-phosphate
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7.5
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dephosphorylation of [acetyl-CoA carboxylase]-phosphate
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brenda
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brenda
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brenda
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brenda
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brenda
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pancreatic beta-cell, normal islets and islets derived from the diabetic Goto-Kakizaki rat
brenda
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brenda
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physiological function
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in procyclic forms ofTrypasnosoma brucei, supplementation of media with the fatty acid stearate or lipids leads to 32.9fold increase in phosphorylation of acetyl coenzyme A carboxylase. Phosphorylation inhibits acetyl coenzyme A carboxylase activity
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C0RGR5_BRUMB
Brucella melitensis biotype 2 (strain ATCC 23457)
334
0
36782
TrEMBL
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C4WH30_9HYPH
330
0
35797
TrEMBL
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C0G3Y3_9HYPH
344
0
37827
TrEMBL
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200000 - 250000
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gel filtration
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monomer
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1 * 71000, SDS-PAGE
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Ethanol
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stable in presence of ethanol over long periods of time
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4°C, stable for several weeks
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medicine
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in pancreatic islets derived from diabetic rats, marked reduction of magnesium- and glutamate-sensitive enzyme activity
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Ingebritsen, T.S.; Stewart, A.A.; Cohen, P.
The protein phosphatases involved in cellular regulation. 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissues. An assessment of their physiological roles
Eur. J. Biochem.
132
297-307
1983
Rattus norvegicus
brenda
Thampy, K.G.; Wakil, S.J.
Activation of acetyl-CoA carboxylase
J. Biol. Chem.
260
6318-6323
1985
Rattus norvegicus
brenda
Krakower, G.R.; Kim, K.H.
Purification and properties of acetyl-CoA carboxylase phosphatase
J. Biol. Chem.
256
2408-2413
1981
Rattus norvegicus
brenda
Shiao, M.S.; Drong, R.F.; Porter, J.W.
The purification and properties of a protein kinase and the partial purification of a phosphoprotein phosphatase that inactivate and activate acetyl-CoA carboxylase
Biochem. Biophys. Res. Commun.
98
80-87
1981
Rattus norvegicus
brenda
Palanivel, R.; Veluthakal, R.; McDonald, P.; Kowluru, A.
Further evidence for the regulation of acetyl-CoA carboxylase activity by a glutamate- and magnesium-activated protein phosphatase in the pancreatic beta cell: defective regulation in the diabetic GK rat islet
Endocrine
26
71-77
2005
Rattus norvegicus
brenda
Ray, S.; Wilkinson, C.; Paul, K.
Regulation of Trypanosoma brucei acetyl coenzyme A carboxylase by environmental lipids
mSphere
3
e00164
2018
Trypanosoma brucei
brenda
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3.1.3.44 [acetyl-CoA carboxylase]-phosphatase
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